CAZyme Information: MGYG000003237_01681

Basic Information

• Species: Victivallis sp002998355
• Lineage: Bacteria; Verrucomicrobiota; Lentisphaeria; Victivallales; Victivallaceae; Victivallis; Victivallis sp002998355
• CAZyme ID: MGYG000003237_01681
• CAZy Family: CBM9
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
645		71681.32	7.2093

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003237	4618450	MAG	United States	North America

• Gene Location: Start: 46490; End: 48427 Strand: +

Full Sequence      

MLSRMRRILAGVAAALLALPAANAAAETEKELQPYAEAAAGAAARYDALKRKGGEAKCGP
DLIGTLRERAGKNIVYPLLYSPKKRMQGSVESWNDIPAVGQLSFLNTSHAALPPGLEAYF
KAAVSDDTLYVLAVAKDSHVNFGFRPAYNSDCFELFLDPFFTRDTRSDDSSMQLFITAAD
PAGKTFRSEGKIPAEARPVPVEGGWGVEIAIPLDNAYFRLKPFDGLAFGFNLSYNNNDDG
KARNQKITWSGLDRNDSSWNNPSVFGVMEVVRTDAQPVEPVRPGPAIEENRRRRSAGETF
EDLGALARSRPSPAVVRGFMSGRLDNGRAFHDMANDWGANAVRLQLHGIGPKPTWTPENY
PVFLDRLEAAVKQAKAAGIKVIPVAFEVPCELGGREMWEVPGVEEGFKRYWRGIAERLKP
YAGTIWGYDLYNEPLGRSQLPYAPVEWRQMAVNIMKAIREVDKDVWIIYETGPGGGWRGF
EDLKPLPDSRVIYSLHFYEPGAFTHQGIAATQLQDPGLLARAQESTGVEYPAFIGGIRFD
EASLERSLRPVIEFQEKYKVPIYVGEFSVIAWAPVDSAVRYLRDVTGIFNRHGWSWTYHA
FREYPGWSLEHEDGVVRKDAALKPVRESARGKVMKEAFRAPVVNK

Enzyme Prediction     

No EC number prediction in MGYG000003237_01681.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH5	330	607	2.7e-37	0.7345454545454545
CBM9	110	268	2e-23	0.8571428571428571

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam00150	Cellulase	7.61e-25	326	598	25	265	Cellulase (glycosyl hydrolase family 5).
pfam06452	CBM9_1	5.56e-22	91	271	7	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	1.20e-17	118	271	39	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.
cd09619	CBM9_like_4	9.88e-14	111	266	31	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.
cd09620	CBM9_like_3	3.11e-08	91	256	8	191	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 may co-occur with various other domains.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AVM43770.1	1.23e-286	12	640	7	633
AVM45119.1	3.16e-246	1	348	15	362
AVM45140.1	2.79e-224	340	645	4	309
AVM45141.1	4.24e-100	302	639	293	632
AVV54443.1	4.99e-85	313	639	42	378

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3AMC_A	3.45e-20	404	601	108	288	Crystalstructures of Thermotoga maritima Cel5A, apo form and dimer/au [Thermotoga maritima MSB8],3AMC_B Crystal structures of Thermotoga maritima Cel5A, apo form and dimer/au [Thermotoga maritima MSB8],3AMD_A Crystal structures of Thermotoga maritima Cel5A, apo form and tetramer/au [Thermotoga maritima MSB8],3AMD_B Crystal structures of Thermotoga maritima Cel5A, apo form and tetramer/au [Thermotoga maritima MSB8],3AMD_C Crystal structures of Thermotoga maritima Cel5A, apo form and tetramer/au [Thermotoga maritima MSB8],3AMD_D Crystal structures of Thermotoga maritima Cel5A, apo form and tetramer/au [Thermotoga maritima MSB8],3MMU_A Crystal structure of endoglucanase Cel5A from the hyperthermophilic Thermotoga maritima [Thermotoga maritima],3MMU_B Crystal structure of endoglucanase Cel5A from the hyperthermophilic Thermotoga maritima [Thermotoga maritima],3MMU_C Crystal structure of endoglucanase Cel5A from the hyperthermophilic Thermotoga maritima [Thermotoga maritima],3MMU_D Crystal structure of endoglucanase Cel5A from the hyperthermophilic Thermotoga maritima [Thermotoga maritima],3MMU_E Crystal structure of endoglucanase Cel5A from the hyperthermophilic Thermotoga maritima [Thermotoga maritima],3MMU_F Crystal structure of endoglucanase Cel5A from the hyperthermophilic Thermotoga maritima [Thermotoga maritima],3MMU_G Crystal structure of endoglucanase Cel5A from the hyperthermophilic Thermotoga maritima [Thermotoga maritima],3MMU_H Crystal structure of endoglucanase Cel5A from the hyperthermophilic Thermotoga maritima [Thermotoga maritima],3MMW_A Crystal structure of endoglucanase Cel5A from the hyperthermophilic Thermotoga maritima [Thermotoga maritima],3MMW_B Crystal structure of endoglucanase Cel5A from the hyperthermophilic Thermotoga maritima [Thermotoga maritima],3MMW_C Crystal structure of endoglucanase Cel5A from the hyperthermophilic Thermotoga maritima [Thermotoga maritima],3MMW_D Crystal structure of endoglucanase Cel5A from the hyperthermophilic Thermotoga maritima [Thermotoga maritima]
3AZR_A	2.07e-19	404	601	108	288	DiverseSubstrates Recognition Mechanism Revealed by Thermotoga maritima Cel5A Structures in Complex with Cellobiose [Thermotoga maritima MSB8],3AZR_B Diverse Substrates Recognition Mechanism Revealed by Thermotoga maritima Cel5A Structures in Complex with Cellobiose [Thermotoga maritima MSB8],3AZS_A Diverse Substrates Recognition Mechanism Revealed by Thermotoga maritima Cel5A Structures in Complex with Mannotriose [Thermotoga maritima MSB8],3AZS_B Diverse Substrates Recognition Mechanism Revealed by Thermotoga maritima Cel5A Structures in Complex with Mannotriose [Thermotoga maritima MSB8],3AZT_A Diverse Substrates Recognition Mechanism Revealed by Thermotoga maritima Cel5A Structures in Complex with Cellotetraose [Thermotoga maritima MSB8],3AZT_B Diverse Substrates Recognition Mechanism Revealed by Thermotoga maritima Cel5A Structures in Complex with Cellotetraose [Thermotoga maritima MSB8],3AZT_C Diverse Substrates Recognition Mechanism Revealed by Thermotoga maritima Cel5A Structures in Complex with Cellotetraose [Thermotoga maritima MSB8],3AZT_D Diverse Substrates Recognition Mechanism Revealed by Thermotoga maritima Cel5A Structures in Complex with Cellotetraose [Thermotoga maritima MSB8]
3AMG_A	2.07e-19	404	601	108	288	Crystalstructures of Thermotoga maritima Cel5A in complex with Cellobiose substrate, mutant form [Thermotoga maritima MSB8],3AMG_B Crystal structures of Thermotoga maritima Cel5A in complex with Cellobiose substrate, mutant form [Thermotoga maritima MSB8]
1CEC_A	1.75e-18	397	598	105	315	ChainA, ENDOGLUCANASE CELC [Acetivibrio thermocellus]
1CEN_A	4.25e-18	397	598	105	315	ChainA, CELLULASE CELC [Acetivibrio thermocellus],1CEO_A Chain A, CELLULASE CELC [Acetivibrio thermocellus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P0C2S3	9.60e-18	397	598	105	315	Endoglucanase C OS=Acetivibrio thermocellus OX=1515 GN=celC PE=1 SV=1
A3DJ77	3.13e-17	397	598	105	315	Endoglucanase C OS=Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) OX=203119 GN=celC PE=3 SV=1
P23340	3.13e-17	397	598	105	315	Endoglucanase C307 OS=Clostridium sp. (strain F1) OX=1508 GN=celC307 PE=1 SV=1
P16169	3.61e-12	323	593	26	285	Cellodextrinase A OS=Ruminococcus flavefaciens OX=1265 GN=celA PE=3 SV=3
P25472	1.01e-08	342	595	77	293	Endoglucanase D OS=Ruminiclostridium cellulolyticum (strain ATCC 35319 / DSM 5812 / JCM 6584 / H10) OX=394503 GN=celCCD 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
0.000352	0.998878	0.000192	0.000213	0.000194	0.000165

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003237_01681.