CAZyme Information: MGYG000004248_00843

Basic Information

• Species: CAG-170 sp000436735
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Oscillospiraceae; CAG-170; CAG-170 sp000436735
• CAZyme ID: MGYG000004248_00843
• CAZy Family: GH110
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
2196	MGYG000004248_6|CGC1	238551.97	4.3281

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004248	2100411	MAG	United Kingdom	Europe

• Gene Location: Start: 61926; End: 68516 Strand: +

Full Sequence      

MKKDIRRERCGSKRKRSALTRLLSLALGLVLVLSCAGGALAAGPAEDLSKPDSPWDHYPA
TDGLSTDKLQSYTPSGNWVFAQAPAGTTSFTVMDELYYVSVESYQKWAVTTGVSGSYDPD
AAVVYWGNSHFFSDGQIMYSGKMPAMIYTAPKSGTISIAAAAKIYVPWWDASEWGGESPN
GMRIAVYKSNQSGTIIPVWPVGERWKLLGGSAGADGTDGHEYEFQPYEICIQAGEKLYFV
MDCNGSELDDQIYWSPTVAYVNDTYDAGNDPALALPEAAVLKDAIPFNGSGDNTYDHGNG
WRFNAAEGDTYRRMNQLGWNVEWTNARYFYSENPNSELDGSDAMEIPWENGVITVDAGVK
NDQWVCNAVCLSPAADGKDVALSYLAPRDGVLKLRFDYADFWQGEGSNQIKLAVYKNNVQ
IWPETGSYIVQSDAAAWETTVLKLDDVVSAARAGDVFHIRASLMESGSEYGLNILPSAEY
TSLEYDANLDKEYQFTSKAHYSYKEQFSGTQGKDSWYYLYAPIGENEATQLPAYYSDWAM
WYSGDLDSYNVPQMFNSELLPGSMYDAIIAFKAPYTGTLKLYMEDGMWLADSTGASDAGD
GCYYGVQLSSDGIVTDLLPLTYIPNGGKVDFQPMLLSVKKNEYIYFRVNRGEANNWHDSL
SLSPAIDYAEIDFDDPGIEEGQAEMRRMPTPGSSLKDDEFPTAARDYTDAKVYKITADEL
MKRITGGKLEAGAVYELTDHGGLYFGGISEPTVYDLQNICIRMSPSGHAWEWPTEEADGR
FAIFVEGTSAALTLRNFTLEVSKWDGSDVQPEAAVNTWNCAGLTLQNVQITGTAGYAVHT
SNGTPLSLSGCRIDGAFANGAVVHEGSEASVTGSFIRNTAAGAAAVEDFGGTGAFVMNNI
LSANGTAVKLHSSDAVVQSNTVTGEIDLGDDLVNTLAALNRTTGAITAKNGKNTVILMNE
AGSLSADGGVSLTLVKNTVAGGASARNVSYLLMQGNTFSGAVNTSGSTDAYGDDLFDPTV
RKENGVNEDLLPKTNVEVFTGMTHKTGVRTENGVQTLKRYLNVSARSNTYAIVPPGLYTA
DALALAGIESYDVYAYGVDVEFKSYSGNVFTMSGCKDIGVFGMYISHINNANGQATIVER
TDEYVIAQTDPGYLPDLTDEKYYPADSRYVEAFHPGQTVPFADIEFSSIEYLGDGRHKCT
FGSANSRELAVGGKITLRGSGTSVVVLTDCDGVRFEDFSIISGAGFGFQERNGEGGTELY
RVAITTKAAPVLPEGFDTSKYADGLIWTDAEGRLRGPQPLLSTCDATHSTNMRRGPQVVN
CLFEKMTDDATNISGEFGCVTGANAETRQITYKKGDNYYEGLPAEFRVGDTAVLFTRAGE
LLATAKVEAVESAGYQVYRLTLDQAVTIKSGTLIENLSANGAGFLFDNCLVDTTRARGFL
LKAPGGAIRHCTIRNTGMAAILVRPEIDDGWNECGYVQELEITDNLLENNGFFKNQPKGS
PIAIAGDGQVTSDPAYLMHQDILIEGNVVRERCTDYALYINGAQRVKVLNNDFGARKGEA
ADTASSVRVDGVYDVELSDNTYPSGAQPRITITAQSRKVYGTDVDSLPIGNYAVLSADTV
YTESGWQLELTIENISDTRQTFDMRFADTTTAGLLPDGQKIPSVTLAAGERRKLYFPVKT
LPGELSPRQTYAQVDVYVSTDGAGGVYNLQATFNAAIKADGTEIQWQRAAAIGKEGTDRG
ESLAADARFAWDENNLYLKVDVTDDVQFDCLNKDELWDWDSLQIGFAPDRTDNSRYFVFT
IGRYNGKVRMFMDNDTIGSREGKAMSTNLLPAAITRDEQTQTTTYELTISWSKFFGLSEA
PAGKTIGFDIVVNDRDEAITEGKEPGQWSRYFIEYYGGIASGRHPEKFGSLILLDGAFTL
PDADVSALNEALAEAKSIDTSAYTEETVKALEEAIRTAEALLAEAPAADRQNEVDEAVKA
LRDSIDALQKRQEEPKPTPAPVQPGKGNGTGGKNDDPFRDVSKNDWYHDAVAYVYENGLM
SGTSRTEFSPNSATTRGMIVTILWRQAGKPVVNYAMRFEDVASGSYYEEAVRWAASIGVV
NGYSETAFGPADPITREQLAAILYRYAKYQDKDVTASASLDSFSDAASVSGYALDAMRWG
CGMKLINGANGKLDPTGLATRAQVAAILQRYCENVE

Enzyme Prediction     

No EC number prediction in MGYG000004248_00843.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH110	1302	1580	1.3e-34	0.5036496350364964
CBM9	1722	1878	5.6e-18	0.8186813186813187

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd09621	CBM9_like_5	4.48e-28	1743	1913	28	188	DOMON-like type 9 carbohydrate binding module. Family 9 carbohydrate-binding modules (CBM9) play a role in the microbial degradation of cellulose and hemicellulose (materials found in plants). The domain has previously been called cellulose-binding domain. The polysaccharide binding sites of CBMs with available 3D structure have been found to be either flat surfaces with interactions formed by predominantly aromatic residues (tryptophan and tyrosine), or extended shallow grooves. CBM9 domains found in this uncharacterized heterogeneous subfamily are often located at the C-terminus of longer proteins and may co-occur with various other functional domains such as glycosyl hydrolases. The CBM9 module in these architectures may be involved in binding to carbohydrates.
cd09619	CBM9_like_4	5.04e-13	1716	1877	1	162	DOMON-like type 9 carbohydrate binding module. Family 9 carbohydrate-binding modules (CBM9) play a role in the microbial degradation of cellulose and hemicellulose (materials found in plants). The domain has previously been called cellulose-binding domain. The polysaccharide binding sites of CBMs with available 3D structure have been found to be either flat surfaces with interactions formed by predominantly aromatic residues (tryptophan and tyrosine), or extended shallow grooves. CBM9 domains found in this uncharacterized heterogeneous subfamily are often located at the C-terminus of longer proteins and may co-occur with various other domains.
cd00241	DOMON_like	2.53e-12	1736	1878	11	150	Domon-like ligand-binding domains. DOMON-like domains can be found in all three kindgoms of life and are a diverse group of ligand binding domains that have been shown to interact with sugars and hemes. DOMON domains were initially thought to confer protein-protein interactions. They were subsequently found as a heme-binding motif in cellobiose dehydrogenase, an extracellular fungal oxidoreductase that degrades both lignin and cellulose, and in ethylbenzene dehydrogenase, an enzyme that aids in the anaerobic degradation of hydrocarbons. The domain interacts with sugars in the type 9 carbohydrate binding modules (CBM9), which are present in a variety of glycosyl hydrolases, and it can also be found at the N-terminus of sensor histidine kinases.
pfam06452	CBM9_1	2.42e-08	1743	1877	31	152	Carbohydrate family 9 binding domain-like. CBM9_1 is a C-terminal domain on bacterial xylanase proteins, and it is tandemly repeated in a number of family-members. The CBM9 module binds to amorphous and crystalline cellulose and a range of soluble di- and monosaccharides as well as to cello- and xylo- oligomers of different degrees of polymerization. Comparison of the glucose and cellobiose complexes during crystallisation reveals surprising differences in binding of these two substrates by CBM9-2. Cellobiose was found to bind in a distinct orientation from glucose, while still maintaining optimal stacking and electrostatic interactions with the reducing end sugar.
pfam00395	SLH	7.16e-08	2078	2119	1	42	S-layer homology domain.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QTH41961.1	8.67e-269	21	2190	4	2332
ARE59829.1	1.76e-41	2017	2195	784	964
QQR06511.1	1.76e-41	2017	2195	784	964
QCI60723.1	2.81e-41	2015	2190	390	565
BCK83697.1	4.78e-41	2015	2195	350	530

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7JW4_A	7.31e-07	1225	1530	270	543	Crystalstructure of PdGH110B in complex with D-galactose [Pseudoalteromonas distincta],7JW4_B Crystal structure of PdGH110B in complex with D-galactose [Pseudoalteromonas distincta]
7JWF_A	2.86e-06	1225	1530	270	543	Crystalstructure of PdGH110B D344N in complex with alpha-(1,3)-galactobiose [Pseudoalteromonas distincta],7JWF_B Crystal structure of PdGH110B D344N in complex with alpha-(1,3)-galactobiose [Pseudoalteromonas distincta],7JWF_C Crystal structure of PdGH110B D344N in complex with alpha-(1,3)-galactobiose [Pseudoalteromonas distincta],7JWF_D Crystal structure of PdGH110B D344N in complex with alpha-(1,3)-galactobiose [Pseudoalteromonas distincta]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
C6CRV0	1.03e-17	2018	2190	1283	1457	Endo-1,4-beta-xylanase A OS=Paenibacillus sp. (strain JDR-2) OX=324057 GN=xynA1 PE=1 SV=1
P19424	2.10e-16	2017	2188	40	210	Endoglucanase OS=Bacillus sp. (strain KSM-635) OX=1415 PE=1 SV=1
P38537	5.15e-08	2029	2196	45	210	Surface-layer 125 kDa protein OS=Lysinibacillus sphaericus OX=1421 PE=3 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
0.012317	0.648080	0.334788	0.002795	0.001187	0.000815

TMHMM  Annotations     

start	end
21	43