CAZyme Information: MGYG000001542_03674

Basic Information

• Species: Paenibacillus_A sp900069005
• Lineage: Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus_A; Paenibacillus_A sp900069005
• CAZyme ID: MGYG000001542_03674
• CAZy Family: GH39
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1085	MGYG000001542_38|CGC5	115273.93	4.863

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001542	5846629	Isolate	not provided	not provided

• Gene Location: Start: 385809; End: 389066 Strand: -

Full Sequence      

MFMKKWMIRLVLVLLVSVSIIPGAAPRAAAAQPQAEVILSSPPIYQGVNRAWPGDADKDP
THAATTRKGTACWTTSQDPLNPYLYVDVESTVKPADATYAIVSVDYYDAAATTVAIEYDG
QNNAYQATPWMPTSGSQTWKNQIFELKGIKFANRTNGADFRLRVHSINGVMPEICFARIQ
VTFATTPTLSVMNPSLLFTTQSANLDFGTVGDSVSYEIADDQGASLRTGSIPVGANGHAP
LSVQDLGPGFYNLTFSSVIDDHPITRTTTFGIVTPTPAGALSPDSFFGIDTHFGHYKALE
GGLMNALATIGYGHIRSDVNWSLIEKQPGVYNWAGYDFEARSQQALELGMTPQGVLAYSN
ANYDNGKTPSSEEGLAAFGQFGKAAAEHYKGKVSDFNVYNEFNGTGFNNGACGTSAACYV
QMLQAMYGPIHEGNPDANVIGPIPSTIDDNWNNAFFAANGIKYMDTFATNVYGYALEGAN
TPPERTLLVSKLPALVQQVKQEAGDRHVPVWITENGWPTYAAASTEQQQADNLVRAQVLA
RAAGVDVFSWYSAMDDGTDPNNREHHFGLFRQPVDGVVGVAPKPGAVTNAVLIRAVTGKG
IEARESLGSDTAYSYPYTGGGSTTRVMWSTGSESAALNTTQPLIVTNEYGAIKTVNPTNG
KIILTLNGSPIYVTGEVDSLGVTQSALSMKVVGQPIKGDAISVTVTADRSNPKTDLPNEL
TLIASGAQPVKLRTSPGKATSATINVPASLLLGQRTIAVDVTKVKPGKGGKDKHEPSLVA
GLRATTHVVKPFEISVQPTITSKATSRSYFLDLDLKNNRNQAFTATQVTYQVGPVSGELT
DAVQIAANGMVSMRVPLPDVPLFDALSYSVTVASGNGSDISAGSISYSPIELADQYTLPA
IDLASQAAWVSLSGTRSSNSDLSGQLRITYNSDGLIIDAVITDDKHFGARAPDALWQTDS
IQFSTYDRVPGQEGGQRVEIGAALLDSGPSVYTFAAPDGQQPGPTPGAQADIVQDGSTMH
YVISVPWASLGFNGPPMQPLGISFLVNDDDQGSSGDSRDGFLQWGSGVGTTPKNPALFRH
AQLVQ

Enzyme Prediction     

No EC number prediction in MGYG000001542_03674.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH39	327	574	7.4e-21	0.6241299303944315

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd09621	CBM9_like_5	4.57e-32	899	1083	1	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	4.54e-05	899	1078	2	186	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	5.42e-05	905	1084	10	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.
cd00241	DOMON_like	8.27e-05	907	1055	3	153	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.
PLN00197	PLN00197	0.001	304	358	133	186	beta-amylase; Provisional

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AZS15277.1	0.0	1	1085	1	1085
QOR71608.1	2.78e-248	25	1084	2	1077
SDS89296.1	1.31e-106	209	1083	229	1086
QJD82799.1	6.59e-96	223	1084	447	1282
AJY74277.1	1.03e-94	186	1079	212	1083

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5JVK_A	2.90e-18	311	683	129	506	Structuralinsights into a family 39 glycoside hydrolase from the gut symbiont Bacteroides cellulosilyticus WH2. [Bacteroides cellulosilyticus],5JVK_B Structural insights into a family 39 glycoside hydrolase from the gut symbiont Bacteroides cellulosilyticus WH2. [Bacteroides cellulosilyticus],5JVK_C Structural insights into a family 39 glycoside hydrolase from the gut symbiont Bacteroides cellulosilyticus WH2. [Bacteroides cellulosilyticus]

Swiss-Prot Hits     

has no Swissprot hit.

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
0.000325	0.998817	0.000326	0.000189	0.000162	0.000142

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001542_03674.