CAZyme Information: MGYG000002702_01354

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae
• CAZyme ID: MGYG000002702_01354
• CAZy Family: GH110
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1230	MGYG000002702_90|CGC1	131773.47	4.0695

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002702	2615547	MAG	Canada	North America

• Gene Location: Start: 46; End: 3738 Strand: +

Full Sequence      

MNNAITAKGTAVQLGCSEAVVQNNVIAGGVEISDGLQNVLVALNQVTGGIGVLNGKNTVI
LLNKVDSIAATGGVSLMLAENTVSGGVSAQKVDYLLMQDNAVTGEILTTDSTNTYGDDLF
DPDVRKENGVNEELLPKTNVEVFAGMTHKTTVRTEDEVQTLKRYLNLSARNNTYAIIPPG
LYTADALALAGVENYDVYAYGVTVEFESYEGNVFTMNNCSDVTVYGMYISHVNNANGQAT
IIEKGDNYVIAQTDPGYLPDLTDETYYPTGSPYVEAFRPGETVPFADIGFQSIEYLGDGK
HKCILTNDRGQELEVGGKITMRGNGTSVVVLTGCGNVRFEDFSIISGAGFGFQERNGDGG
TQLYRVAITPKAAPVLAEDFDTSKYSADLIWTDDEGRLRGPNPLLSTCDATHSTNMRKGP
QVVNCLFEKMTDDATNISGEFGKVTDYDPATRKLTYTKGDNYYEGLPANFQAGDTAVLFT
RGGELLATAKVTAEPESGGWQVYILTLDQDVEIKSGTLIENISANGAGFLFDNCLVDTTR
SRGFLLKAPDGAINNCTIRNVGMAAILVKPEIDEAWNECGYVQNLEITNNIFENTGFFNN
TLKGSPVAISGDGQFTADPAFLMHQDILIQNNIIKDRNTDYAVYVNGAQRVKLLDNDFGA
RKGYTAETDTASSVRIDGAYDVEVSGNVYPAGAEPRVDMTAQTRKIYGADIEQQPIGNYA
IVSAASVYTTEGWQVELTIENIFDETVTYTLAFADSTSKGLLADGTKIPTVTLDPGETRK
LYFPVQTLPGDMVPKQTYAQTDVAVSVPSGSQGVFTNQISFNGAINVPSEDALDWTQAPG
IGKEGTDRGEYIASDARFAWDSDNLYMRVVVTDDVHYDCANLGEFYDWDSLQIGFIPDRK
NLEGYFVYFIGLIDGKAKLQMDTTTLSGIDLGDITASVSRDDDAQTTTYLMAIPWSLFGI
EAPAGESIGFEIVVNDRDGPIVEGQEPEQWNRYFLEYYGGIAVSKNRALYGSLTLLDEPF
VIPSADTSDLEAAIADAEKVDASLYTEASVKALNDAVNAAKSLLESKPIVNAQDDVDAAA
KAIRDAIAALVKPADTSDLETAIADAGKVDASLYTEASVKALNDAVKAAEALLESKPTED
NQDDVDAAVKAIRDAIAALEKLPESNPGSSSGTPSSSEAPSSSETPSSGEEPSTGSAPHT
LAIFLLSALSAIALLAGLLLRRARGNSSRV

Enzyme Prediction     

No EC number prediction in MGYG000002702_01354.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH110	406	687	1.4e-31	0.5036496350364964

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd09621	CBM9_like_5	2.12e-26	856	1015	32	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.
cd00241	DOMON_like	2.20e-11	832	979	2	149	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.
cd09619	CBM9_like_4	3.15e-10	853	980	37	163	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.
pfam06452	CBM9_1	3.16e-06	856	979	35	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.
pfam07554	FIVAR	4.21e-06	1099	1160	3	69	FIVAR domain. This domain is found in a wide variety of contexts, but mostly occurring in cell wall associated proteins. A lack of conserved catalytic residues suggests that it is a binding domain. From context, possible substrates are hyaluronate or fibronectin (personal obs: C Yeats). This is further evidenced by. Possibly the exact substrate is N-acetyl glucosamine. Finding it in the same protein as pfam05089 further supports this proposal. It is found in the C-terminal part of Bacillus sp. Gellan lyase, which is removed during maturation. Some of the proteins it is found in are involved in methicillin resistance. The name FIVAR derives from Found In Various Architectures.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QTH41961.1	2.28e-170	56	1018	899	1884
SDT96813.1	1.07e-28	177	658	19	512
CCW36343.1	1.44e-26	177	658	75	549
QDU56661.1	3.88e-22	169	658	57	541
SHH19418.1	6.16e-20	170	659	85	572

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7JW4_A	3.75e-07	406	635	318	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	1.47e-06	406	635	318	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
B1KD83	2.99e-07	406	687	307	580	Alpha-1,3-galactosidase A OS=Shewanella woodyi (strain ATCC 51908 / MS32) OX=392500 GN=glaA PE=3 SV=1
A6L2M8	2.02e-06	398	654	289	583	Alpha-1,3-galactosidase B OS=Phocaeicola vulgatus (strain ATCC 8482 / DSM 1447 / JCM 5826 / CCUG 4940 / NBRC 14291 / NCTC 11154) OX=435590 GN=glaB2 PE=3 SV=1

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
0.999972	0.000084	0.000001	0.000000	0.000000	0.000000

TMHMM  Annotations     

start	end
1198	1220