CAZyme Information: MGYG000002683_01949

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia; RUG12999; RUG12999
• CAZyme ID: MGYG000002683_01949
• CAZy Family: GH74
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1272	MGYG000002683_158|CGC1	141904	4.6586

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002683	3225682	MAG	Canada	North America

• Gene Location: Start: 2358; End: 6176 Strand: +

Full Sequence      

MKKILCFLIAAAMLCLPSYAKEYSNTVKLTAETEKSAAESLVFRVNNNSCFIKGMRCAVD
ESNPKIAPFAENGAVYVPLDICTETFGTKPETEVKIKYKTEFADAEAVAQKLGKKYYTDG
KLAVISENEISAKSAKELSDALEYKWQNVWLGMEGFVTGMVTHPKDPDLIYARTDVGGAY
RWNAKGQRWIPMTDCISHEDIWLNCVAGIAVDPSDVNTVYIACGAYTYTTPYDVLKSTDK
GKTWKRTNLNKMQLGEGDHRYSGEPIAVDPNNSNRVFCGTYRDGLWYSEDGAETWKRVES
IPNTSQVVSGGVRIVYFDENSEVKDGKTSVVYAGVYGEGIYKSTDGGMSFSKIPDSPEVP
LRFTISEGEVVVSATHRSASKKVKTGLFIYDGKTWNNISPTWKDEYKSVGGFMIDRENPN
FIVAAGAPYTDNLGYFMRSYDRGKTWENMGFPRGENNIWTNPSCIIQDGRNPNKIILPNG
AGIHMVEDVHAANFYSKYMETGGEELVCAKVMSIPDRRAPLYSVACMDRGFSKSNRIDVR
PEAQDSEAWMETHAMDFCEENPKFVVRVGNYNGGVAAYSEDYGNTYHAMNWDKKYGCVNV
ALSPTVKENGYPVMLMSAGDGKKGTLWRSWDFGKTWEQLDADFLQQKSPGQERIILLSDR
VDGKTFYYCDDGSFYVSTDCGTTWTKKQQFKYPSRWGENNRYYATIPGIEGGVWIKTIDG
IYETYDKGSSWSLISSVKNPVGFGFGKGKSSSNIPAAYVVGEIDGIYGIYISDDLGKNWR
RIDGGFNLPCSILQITGDRNVYGRLFIATAGRGVFVGQSDEIDDMPPLITLENESCTDEK
GLSYALENKKFTVKGSVDEPAEVRINSNKVEVSADGEFEYTLDLNYGDNTIYVEAADMHG
NKSETVYLKERYLPDYVPVEYTVGEDILTREKTVKITGKTLPEAVVYCGGSVFKADSKGN
FEAVYNTEQEKSAVAVYAESKSGSVSETKVFNVTYDSHIPIIEMEEAPKSVEGGFAILKG
KLNEPGEVRANGKNIIVRNDLSFYVFCMLEKGDNTIKIQARDTAKNVAKPVTLNIKSEGA
ASDKSQITAEYKSDKFDFDGDVGEWNLNYTLEKLLADSPNNLVNFGLMWDEENLYIGVKV
LDDVIFTESGTSFYEDCIEIYIDGDNNKGKRYDEHDAQLIFVPGENYDDARRKYKILDNG
YSMEIVLPWKDFRVSPKAGDSVGFDIDCGDNDNLYTDKRRTGVIGFNGTMNNWASTEDYS
TVTLVGPEDKLE

Enzyme Prediction     

No EC number prediction in MGYG000002683_01949.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CBM9	1124	1264	6.6e-24	0.8241758241758241
GH74	202	308	2.2e-16	0.4592274678111588

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd09619	CBM9_like_4	1.56e-21	1099	1257	5	184	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	3.11e-18	1124	1265	34	182	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.
cd00005	CBM9_like_1	6.85e-18	1127	1265	43	185	DOMON-like type 9 carbohydrate binding module of xylanases. 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. The CBM9 domain frequently occurs in tandem repeats; members found in this subfamily typically co-occur with glycosyl hydrolase family 10 domains and are annotated as endo-1,4-beta-xylanases. CBM9 from Thermotoga maritima xylanase 10A is reported to have specificity for polysaccharide reducing ends.
cd15482	Sialidase_non-viral	1.73e-10	186	406	56	304	Non-viral sialidases. Sialidases or neuraminidases function to bind and hydrolyze terminal sialic acid residues from various glycoconjugates, they play vital roles in pathogenesis, bacterial nutrition and cellular interactions. They have a six-bladed, beta-propeller fold with the non-viral sialidases containing 2-5 Asp-box motifs (most commonly Ser/Thr-X-Asp-[X]-Gly-X-Thr- Trp/Phe). This CD includes eubacterial and eukaryotic sialidases.
cd00241	DOMON_like	1.20e-09	1116	1243	13	157	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ANE48490.1	9.62e-158	143	1264	37	1181
ANE48489.1	1.06e-120	134	1266	28	1114
QZN78306.1	1.90e-102	134	817	24	716
QJC51548.1	4.73e-102	144	1264	40	1353
APO44368.1	3.09e-93	138	817	28	703

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6P2M_A	1.89e-82	144	817	10	691	ChainA, Type 3a cellulose-binding domain protein [Caldicellulosiruptor lactoaceticus 6A]
4LGN_A	1.36e-76	144	817	7	733	Thestructure of Acidothermus cellulolyticus family 74 glycoside hydrolase [Acidothermus cellulolyticus 11B]
6P2N_A	6.95e-73	144	813	6	741	Crystalstructure of Paenibacillus graminis GH74 (PgGH74) [Paenibacillus graminis]
6MGL_A	5.73e-72	144	813	6	740	Crystalstructure of the catalytic domain from GH74 enzyme PoGH74 from Paenibacillus odorifer, D60A mutant in complex with XXLG and XGXXLG xyloglucan [Paenibacillus odorifer]
2CN2_A	2.95e-71	141	821	8	735	ChainA, BETA-1,4-XYLOGLUCAN HYDROLASE [Acetivibrio thermocellus],2CN2_B Chain B, BETA-1,4-XYLOGLUCAN HYDROLASE [Acetivibrio thermocellus],2CN2_C Chain C, BETA-1,4-XYLOGLUCAN HYDROLASE [Acetivibrio thermocellus],2CN2_D Chain D, BETA-1,4-XYLOGLUCAN HYDROLASE [Acetivibrio thermocellus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q3MUH7	2.83e-74	112	946	5	880	Xyloglucanase OS=Paenibacillus sp. OX=58172 GN=xeg74 PE=1 SV=1
A3DFA0	1.03e-71	141	829	35	770	Xyloglucanase Xgh74A OS=Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) OX=203119 GN=xghA PE=3 SV=1
Q70DK5	3.44e-71	141	829	35	770	Xyloglucanase Xgh74A OS=Acetivibrio thermocellus OX=1515 GN=xghA PE=1 SV=1
Q5BD38	5.67e-57	126	821	19	810	Oligoxyloglucan-reducing end-specific xyloglucanase OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=xgcA PE=1 SV=1
A1DAU0	4.76e-55	122	826	10	810	Probable oligoxyloglucan-reducing end-specific xyloglucanase OS=Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) OX=331117 GN=xgcA 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
0.000778	0.726353	0.272023	0.000291	0.000283	0.000243

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002683_01949.