CAZyme Information: MGYG000004439_01165

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia; UMGS1810; UMGS1810
• CAZyme ID: MGYG000004439_01165
• CAZy Family: CBM9
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1409		153975.41	4.5306

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004439	2174785	MAG	Israel	Asia

• Gene Location: Start: 9719; End: 13948 Strand: -

Full Sequence      

MKKFKRAAAFILCTAMMLGALPAFAADKIGADVIVADAKLSNPYYEVGDLVSISLYIKNI
GDEAMKLGWAGVDNLVGLKSHGSNWNWTRPVIYPGQTIEFVVNAPFEVTDEAISIGARCN
SSPSVTTEPSANQGNNYSTFSFTPIKTKHDLVIKDVSVSDLNFAEGNAVNFDIEYRNIGI
EEIPYGTVSIDLNVNGKNYTFTDVSSVEGRETRKLKTDNIYIEGDSVNVTAYINADETMA
EDNYDNNSFTKTINAAKPGKYGYTWASLRLGGGGAVRDAFIHPKFKDEIYIGSDVNGVFK
FDPYSRMNIPLNETTAKEWENIKFFLEMASAYDNPNILFNAGGNYFNGAVEATSLKCALF
RSFDKGKTWQPLEIPFEYAEESDGSNGTIAIDPNNSNILYSVSVRDGLWKTTNALDRSVK
WERATLPGYTAEMTGKANIASIVFDEKSAVKDGKTQTFYVSADTYGIFKTTDGGNSFELI
STPVSEFQNLFIDKLGRLVASGYNGVFRYDGSEWTDISPLKNTKFRIDVNPNNANMIAAT
NISTIYITVDGGITWKDILKDSTVVNQMPWQPTSWYKDNVQFVRFDPHYNNRLYYGDWFG
AFVIDDPSAEKVAVQDITYGIEELCSRALVCLPEGADTRLVYGAHDVNGLTVDTLFEFPE
NRTEEPGMQETVGIGFAEKQPNFVVRVGGYSRGTGAGNAGYTTDGGKTWTRFPTYPTKSD
GVTYAQNGKVAVSCDFNDDGKPTILATVLNDYVYRSTDLGETWTPVTSLPQKLVERYIDV
SEPVAADKENKDVFYAYDRWTGDFYTSTDGGASFSKKSTIPTGDAYSQVVPVAGKEGHVY
VALSGNGLWYSKNYGATFEKVEGVNNAYGFDLGIKAPCSDEMTMYVLGNVNSNNGVFRST
DLGKTWAKISDEKQQTFWNRIEFLKADRRQFGVVYVASHGNGILTGFPSQLDLVLPRCGI
YNVRDGKTVNKADYTVEGGSTKSGTAYITVNGKATEQKLDENNRYSLTAKLNLGENSISV
YTTDESGQKSNTVNTTVNYDPNYLGLNVNSEGLTTIADAFSILGSINDDPRHTKVYVNGV
QASVDPVTGVFSQSVSLLSGDNPVEVVAVKGSVSEQENVVVKCDREAPTVSFKNLPKVTN
EPLLLLDAVLSEAGSIEVGTYAFDAYSGENPEVKIPIKLTNGENKIEFKLTDLAGNTAVH
KESIFFEGDAVFNSVKTNEAIAYDGTPAIDGVLDDGWMLNRVIADKVADNSNASGVFGLM
ADKNNLYIAVKVYDSKVDDPGLATATSYLADSVEIFFDPEYNRGTKYSGGDQQIRLGLSG
LAYSCTKATSLKTVKTASSRFEDGYIIEAAIPWNVISLEYSRGKKFGFEVSINDSSDGGV
TRDGAVAWSADGNSYCNTSKFGTTYIGSK

Enzyme Prediction     

No EC number prediction in MGYG000004439_01165.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CBM9	1229	1403	2.7e-31	0.978021978021978

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd00005	CBM9_like_1	2.45e-33	1219	1403	1	181	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.
pfam06452	CBM9_1	1.05e-25	1229	1403	1	178	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.
cd09619	CBM9_like_4	1.13e-23	1226	1402	1	187	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	7.05e-09	1236	1385	1	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.
cd15482	Sialidase_non-viral	7.46e-08	701	842	178	321	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ANE48490.1	5.50e-121	255	1409	30	1184
ANE48489.1	1.04e-98	255	1406	30	1112
QJC51548.1	4.90e-94	262	1408	39	1355
BAY33488.1	4.55e-82	263	948	40	705
BAY25007.1	1.56e-81	263	948	40	705

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6P2M_A	5.12e-76	263	949	10	694	ChainA, Type 3a cellulose-binding domain protein [Caldicellulosiruptor lactoaceticus 6A]
2CN3_A	3.23e-60	263	950	11	733	ChainA, BETA-1,4-XYLOGLUCAN HYDROLASE [Acetivibrio thermocellus],2CN3_B Chain B, BETA-1,4-XYLOGLUCAN HYDROLASE [Acetivibrio thermocellus]
6MGL_A	5.05e-60	263	948	6	746	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	7.82e-60	263	950	11	733	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]
6P2N_A	3.16e-58	263	948	6	747	Crystalstructure of Paenibacillus graminis GH74 (PgGH74) [Paenibacillus graminis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q3MUH7	2.60e-63	263	948	38	766	Xyloglucanase OS=Paenibacillus sp. OX=58172 GN=xeg74 PE=1 SV=1
A3DFA0	2.25e-60	263	950	38	760	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	7.24e-60	263	950	38	760	Xyloglucanase Xgh74A OS=Acetivibrio thermocellus OX=1515 GN=xghA PE=1 SV=1
Q5BD38	3.25e-53	250	944	22	804	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	2.59e-47	255	952	19	804	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
0.000242	0.999007	0.000180	0.000193	0.000174	0.000154

TMHMM  Annotations     

start	end
7	26