CAZyme Information: MGYG000002756_02319

Basic Information

• Species: Blautia sp900765525
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Blautia; Blautia sp900765525
• CAZyme ID: MGYG000002756_02319
• CAZy Family: GH115
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
974	MGYG000002756_43|CGC1	112321.88	5.303

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002756	3762639	MAG	Netherlands	Europe

• Gene Location: Start: 9880; End: 12804 Strand: -

Full Sequence      

MDISFILADREGAADFVLDRDACEGIRRVADKVREDVRKVTGKLPKLTQETGPGFQVLAG
ILEESRMLKELEEEGGDCFQKIRGKRECYAFLVLQGKEGEKPKLVIAGSDKRGCIYGLFH
ISELMGVSPWVTFADVVPKKRQAVIFTRKENRISREPSVKYRGFFLNDEWPALGNWTFEK
FGGFTWQMYDMIFETLLRLKGNYLWPAMWTSSFSLDGPGEENARLADAYGIVMSNSHHEP
CLRHSEEWDMVKGEDSPYGKDWNYLTNKEGLLEYWKDGLKARGKYENIITIGMRGERDSL
LLEEDAGLEKNIGLLKDVIAQQRRLIREYVEKDRGEAPQLFVIYKEVEDYFYGTQGKQDG
LKDWEGLEGVTLMVCEDNYGNLRRMPEEEVRNRKGGWGIYYHFDYHGSPVSYEWVNSSYL
PKIWDQMTAAYEFGVRDIWVVNVGDLKFQEYPLSFFMDLAYDYQTWGVENKKAPGQYLKY
WVEREFGSRMEEKEKALLEEVMAGYTKINHNRKPEAMGPKVYHPVHFGESEKLLEHIREL
EEKLDFLKEKVPGELLPAYWELVYYPARGSLNVQKMNLCAGRNHYFARMRALSANIYGKK
MKECIATDRSLTKEFHNLLERKWNHMGDSRHVGFCHWNDEESGYPLEMVVEPSDAQELAV
YVQGESTWTCGGDWTGKKLFMKQFLEAGVDRAAFVLENRSREPVEFQIESLVPWISFSET
RGKVQERKEILVSVDKTKAREKEGLFYVKYGARKIQIQAEWDYEEIPDCPAGTFLEKDGY
VSIEAEHYTRKQDSAKGGFQLLEGYGKTLSGLKVFPCNQVFQGQDRPSLLYRVYVPQPGT
YELELYCAPVNPLSQRWEVSCSVRVNGGEEKQVFLLPQDFHGGDPGCGPWCEMVLDQIIR
KKVEIRLQAGVNEIEIMGETPGFLLEKLVAVREGKELPHSCLGPEETYRITEEGNVPLSK
KGIFIHFIAQSALL

Enzyme Prediction     

No EC number prediction in MGYG000002756_02319.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH115	5	660	5.2e-205	0.8622668579626973

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam15979	Glyco_hydro_115	2.36e-173	156	515	2	333	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	5.03e-42	773	946	1	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.
pfam03648	Glyco_hydro_67N	0.006	42	120	49	119	Glycosyl hydrolase family 67 N-terminus. Alpha-glucuronidases, components of an ensemble of enzymes central to the recycling of photosynthetic biomass, remove the alpha-1,2 linked 4-O-methyl glucuronic acid from xylans. This family represents the N-terminal region of alpha-glucuronidase. The N-terminal domain forms a two-layer sandwich, each layer being formed by a beta sheet of five strands. A further two helices form part of the interface with the central, catalytic, module (pfam07488).

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
VCV24041.1	0.0	3	950	1	948
CBL13087.1	0.0	6	949	4	949
VCV21315.1	0.0	6	949	4	949
EEU99942.1	0.0	6	949	4	949
QAY66984.1	1.39e-291	10	952	11	967

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6NPS_A	3.49e-290	6	950	12	966	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]
4ZMH_A	5.79e-163	7	949	16	935	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]
7PUG_A	1.21e-115	5	657	17	655	ChainA, xylan alpha-1,2-glucuronidase [uncultured bacterium]
7PXQ_A	6.22e-115	5	657	16	654	ChainA, xylan alpha-1,2-glucuronidase [uncultured bacterium]
4C90_A	2.44e-113	18	639	57	652	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]

Swiss-Prot Hits     

has no Swissprot hit.

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
1.000059	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002756_02319.