CAZyme Information: MGYG000004499_00657

Basic Information

• Species: Victivallis sp900551245
• Lineage: Bacteria; Verrucomicrobiota; Lentisphaeria; Victivallales; Victivallaceae; Victivallis; Victivallis sp900551245
• CAZyme ID: MGYG000004499_00657
• CAZy Family: GH50
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
908	MGYG000004499_4|CGC1	104735.08	8.624

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004499	4071424	MAG	Israel	Asia

• Gene Location: Start: 82424; End: 85150 Strand: -

Full Sequence      

MRFFLFSLLLFSSVQIYSAPILKEDRIEFPVPKLGVLEIFWPGYRAESDDRMLSPKIVEK
GEHHAVLRFPDGDLPDVKITLQNDIIRLEYGSGRTGTLHIRLTFPQRPGRNFSWRIPGKQ
MDFRPLPAVLQEKHHIWRGRASGFEFAEEDIRNVVVTWSRESYCELQDNRKWNWPVFQLD
IFRPVPKKGKRDSLEIHLQAAESKMLRSRKGPVCDRFGQSMKVEWPGKIRRDEELKADLV
SDRAYYRSFTPLATDAFGGKLDSEIHWNAGGFFKLGKYNGHDIFISPDGNPFFQLAVCTV
APCDDYTYVKGREDLYLELPSRKAPFDKAWMNPDVVSFYIANYIRKTGTPFCLAAWKRDV
VYRLRQWGFNSQGAFRDTPELNRKLQFPYCPELPFQGVPCFIADVFDPFSPDVREAIDRN
FRRLKRDASNPVIIGYFSGNERKYSEVAARLLACDGNVAARRELVRFLKERYQGDVERFS
AAWNLPIRNFAELEKIHPDLKTPAAWNDLNEFMDHFFDAYFKLIHDTFRKYDRNHLLLGA
RFLPGQTRVEAAVRAAGKYNDVFSLNYYSYEIENHFLERIHRLSGVPLLLSEWHFGSTEQ
GLAGAIRPVRNQRERALHYRHYVEQAAALPFVVGIQWFSLLDQALTGRWFQKYQGENMNI
GFLNVADRPYRELAAAAAETNGRVYDIIAGKIEPFSRVSGLVRTARQPKKTFIPRAVEGH
KVDGIRSPWPGRPAERLGRLDLVHGDSASVSADFWLCYDQDFLYLYADVADSTPGMNPFS
PALFWQGDAVELFFGPNEITKDGQLRFGDCQLLLSAGGNSRGYWCNRREQPPVKRVVRIW
TDRKGYTMEAAIPWQALGIKPENGTEFRFDLGLDNFDGKQPQECQLMWSGTGRNSEDRTN
WGTAVLVD

Enzyme Prediction     

No EC number prediction in MGYG000004499_00657.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH50	203	685	2e-85	0.7886676875957122
CBM9	747	906	3.8e-22	0.8571428571428571

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd09619	CBM9_like_4	5.09e-23	727	908	13	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.
cd09621	CBM9_like_5	1.42e-12	733	878	1	161	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.
cd00005	CBM9_like_1	3.75e-12	747	907	34	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.
cd00241	DOMON_like	1.77e-09	744	882	12	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.
pfam06452	CBM9_1	4.09e-09	746	907	27	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AVM47142.1	2.49e-263	22	908	23	906
SDU06021.1	2.65e-184	125	906	144	937
SDU02961.1	5.45e-177	69	908	73	940
AHF90550.1	3.34e-174	215	907	2	717
SDT95096.1	1.43e-156	215	907	39	756

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6XJ9_A	1.78e-43	213	686	222	760	Structureof PfGH50B [Pseudoalteromonas fuliginea],6XJ9_B Structure of PfGH50B [Pseudoalteromonas fuliginea]
4BQ2_A	1.62e-40	151	685	138	743	Structuralanalysis of an exo-beta-agarase [Saccharophagus degradans 2-40],4BQ2_B Structural analysis of an exo-beta-agarase [Saccharophagus degradans 2-40],4BQ2_C Structural analysis of an exo-beta-agarase [Saccharophagus degradans 2-40],4BQ2_D Structural analysis of an exo-beta-agarase [Saccharophagus degradans 2-40],4BQ3_A Structural analysis of an exo-beta-agarase [Saccharophagus degradans 2-40],4BQ3_B Structural analysis of an exo-beta-agarase [Saccharophagus degradans 2-40],4BQ3_C Structural analysis of an exo-beta-agarase [Saccharophagus degradans 2-40],4BQ3_D Structural analysis of an exo-beta-agarase [Saccharophagus degradans 2-40]
4BQ4_A	3.84e-40	151	685	138	743	Structuralanalysis of an exo-beta-agarase [Saccharophagus degradans 2-40],4BQ4_B Structural analysis of an exo-beta-agarase [Saccharophagus degradans 2-40],4BQ5_A Structural analysis of an exo-beta-agarase [Saccharophagus degradans 2-40],4BQ5_B Structural analysis of an exo-beta-agarase [Saccharophagus degradans 2-40]
5Z6P_A	2.25e-37	117	685	131	759	Thecrystal structure of an agarase, AgWH50C [Agarivorans gilvus],5Z6P_B The crystal structure of an agarase, AgWH50C [Agarivorans gilvus]
5T3B_A	1.29e-11	245	688	79	476	ChainA, Glycoside Hydrolase [Phocaeicola plebeius],5T3B_B Chain B, Glycoside Hydrolase [Phocaeicola plebeius]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P48840	8.59e-39	213	685	431	949	Beta-agarase B OS=Vibrio sp. (strain JT0107) OX=47913 GN=agaB PE=3 SV=1
P48839	4.23e-26	213	735	398	956	Beta-agarase A OS=Vibrio sp. (strain JT0107) OX=47913 GN=agaA 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
0.000247	0.999161	0.000147	0.000149	0.000133	0.000129

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004499_00657.