CAZyme Information: MGYG000001657_01910

Basic Information

• Species: RC9 sp900760425
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; UBA932; RC9; RC9 sp900760425
• CAZyme ID: MGYG000001657_01910
• CAZy Family: GH115
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
983		110820.42	5.9906

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001657	2980281	MAG	United States	North America

• Gene Location: Start: 2371; End: 5322 Strand: +

Full Sequence      

MKPDRIIFILFLLFQMISAQAQVSLAEKSGRGTFPLAGKTAATVCYDTEDAAVVKTAVEL
FVSDIYKVTGQSAPVVASHKAEGKAQYAVIVGTIGQSSWIDSMVEKGKIDVTEIKGGWER
YAVRMVDNPVKGIRKALVIAGSDRRGTAYGLMSISRTIGVSPWYWWLDAPVAERAQLNLA
VTPFDSKTPSVKYRGVFINDEDWGLLRWAKKNFEKDLGNIGPKTYDKVCELLLRLQANML
APAMHEASTAFYQIPENKEIADRYAIAIGTSHCEPLLLNTASEWFKDRYGEWNYNDNKER
VDSVLKARVTEASPYENVYTLALRGLHDRAMSGNSDLDARKATMQEALLAQRQILVDVLG
KKAEDIPQAFTPYKEVLDVFNRGLELPDDVTIIWPDDNYGYFKRLSSPKEQKRSGRSGVY
YHSSYLGRPHDYLWMNTTSPTMMYEELRKAYDSTADRIWLLNAGDIKSCEFAVEFFLSMA
YDIDAFSYGRSASYRAEWLGGILGMEHYDALQSIFDEFYHQAFIRKPEFMGWGYQWATDK
HGNERNTDTDFSFANYREADRRLAAYARIAGETDRLMEEMPESHKACFYQAVYYPVKACE
LLNRMVLSGQKNRWYAIQNRAATGMAADIARSCHDSLRVITDGYNRLLDGKWDHIMTMGQ
GFASSYFKMPVLRETELAANPAMGIMAENEGSLNGVSSYHLLPAFNTYFRRSHYIDVFNT
GKGELSWNAAADKDWIRLDKVSGKTATEERVEVSVDWSSVPAGRNVRGTVTFTDASGATE
QVLVSVFNPSAPSLEEMKGMYVQNDGYISIDAAGYHRKRENDRIKVITIPNLGVENTAIQ
LGDPMMPKENTRRRDCPLVEYDFYTFEQGSVDVYTYVLPTFVLNADRGYAGHEATNLETQ
YGVCIDEGPVMNPSTSSIEYAQIWYESVLRNCRVNKTTLHINEPGKHTLKILCGDAGTVV
QKIVLDFGGMKRSYLGPEPTKAE

Enzyme Prediction     

No EC number prediction in MGYG000001657_01910.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH115	34	670	1.1e-213	0.8350071736011477

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam15979	Glyco_hydro_115	5.76e-156	187	529	1	334	Glycosyl hydrolase family 115. Glyco_hydro_115 is a family of glycoside hydrolases likely to have the activity of xylan a-1,2-glucuronidase, EC:3.2.1.131, or a-(4-O-methyl)-glucuronidase EC:3.2.1.-.
pfam17829	GH115_C	6.80e-47	801	979	2	172	Gylcosyl hydrolase family 115 C-terminal domain. This domain is found at the C-terminus of glycosyl hydrolase family 115 proteins. This domain has a beta-sandwich fold.
pfam13004	BACON	5.59e-04	726	785	2	59	Putative binding domain, N-terminal. The BACON (Bacteroidetes-Associated Carbohydrate-binding Often N-terminal) domain is an all-beta domain found in diverse architectures, principally in combination with carbohydrate-active enzymes and proteases. These architectures suggest a carbohydrate-binding function which is also supported by the nature of BACON's few conserved amino-acids. The phyletic distribution of BACON and other data tentatively suggest that it may frequently function to bind mucin. Further work with the characterized structure of a member of glycoside hydrolase family 5 enzyme, Structure 3ZMR, has found no evidence for carbohydrate-binding for this domain.
pfam19190	BACON_2	0.001	711	786	16	88	Viral BACON domain. This family represents a distinct class of BACON domains found in crAss-like phages, the most common viral family in the human gut, in which they are found in tail fiber genes. This suggests they may play a role in phage-host interactions.
cd14948	BACON	0.005	726	785	27	81	Bacteroidetes-Associated Carbohydrate-binding (putative) Often N-terminal (BACON) domain. The BACON domain is found in diverse domain architectures and accociated with a wide variety of domains, including carbohydrate-active enzymes and proteases. It was named for its suggested function of carbohydrate binding; the latter was inferred from domain architectures, sequence conservation, and phyletic distribution. However, recent experimental data suggest that its primary function in Bacteroides ovatus endo-xyloglucanase BoGH5A is to distance the catalytic module from the cell surface and confer additional mobility to the catalytic domain for attack of the polysaccharide. No evidence for a direct role in carbohydrate binding could be found in that case. The large majority of BACON domains are found in Bacteroidetes.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QGT72411.1	0.0	16	981	15	981
QDH53391.1	0.0	16	981	15	981
EDO12283.1	0.0	16	981	15	981
QRQ54524.1	0.0	16	981	15	981
ALJ47615.1	0.0	16	981	52	1018

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4ZMH_A	3.45e-144	42	980	23	933	Crystalstructure of a five-domain GH115 alpha-Glucuronidase from the Marine Bacterium Saccharophagus degradans 2-40T [Saccharophagus degradans 2-40],4ZMH_B Crystal structure of a five-domain GH115 alpha-Glucuronidase from the Marine Bacterium Saccharophagus degradans 2-40T [Saccharophagus degradans 2-40]
5BY3_A	7.28e-130	38	653	25	612	Anovel family GH115 4-O-Methyl-alpha-glucuronidase, BtGH115A, with specificity for decorated arabinogalactans [Bacteroides thetaiotaomicron VPI-5482]
6NPS_A	1.94e-98	85	980	61	963	Crystalstructure of GH115 enzyme AxyAgu115A from Amphibacillus xylanus [Amphibacillus xylanus NBRC 15112],6NPS_B Crystal structure of GH115 enzyme AxyAgu115A from Amphibacillus xylanus [Amphibacillus xylanus NBRC 15112]
4C90_A	1.02e-94	64	656	75	640	Evidencethat GH115 alpha-glucuronidase activity is dependent on conformational flexibility [Bacteroides ovatus],4C90_B Evidence that GH115 alpha-glucuronidase activity is dependent on conformational flexibility [Bacteroides ovatus],4C91_A Evidence that GH115 alpha-glucuronidase activity is dependent on conformational flexibility [Bacteroides ovatus],4C91_B Evidence that GH115 alpha-glucuronidase activity is dependent on conformational flexibility [Bacteroides ovatus]
7PUG_A	3.23e-89	47	657	32	626	ChainA, xylan alpha-1,2-glucuronidase [uncultured bacterium]

Swiss-Prot Hits     

has no Swissprot hit.

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
0.000202	0.999185	0.000153	0.000153	0.000138	0.000136

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001657_01910.