CAZyme Information: MGYG000001920_01589

Basic Information

• Species: Phocaeicola sp900546355
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Phocaeicola; Phocaeicola sp900546355
• CAZyme ID: MGYG000001920_01589
• CAZy Family: GH30
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
444		50038.5	4.2815

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001920	3068459	MAG	Denmark	Europe

• Gene Location: Start: 5877; End: 7211 Strand: +

Full Sequence      

MKQLKSFLFLFLASTLFWACSDDDTVNKSLWGDSYARFVRNAMTVTSTEGTAEAIIDWQQ
STWEITLGEGYIVTNVTPTSGGDNNGEHQFTQVTLTCNANTSMDTRTQVIRLTDRNGTTT
ELTITQEWADKADDTDHLKPEHYADYADHLIRYIDFMKQNGVDIYAVSVQNEPDMDFTAW
TPQEVTAFLKQEGARIRETGVKLMSPEACGYQPEYTDAVLNDAEAFAQTDIVAGHLYQGF
TDLSSSYVKDRHDYVCALYPRLGGKTWWMTEHLFNDGETEEDPSLWQFWEWDYNFSHLAK
EIHMCMDGYCSAYVYWYLKRFYGMIGDTDERCKEEEGEVSKNGYILSHYARYATGTTRIA
VTSASENIEATAYLNEATGEVTLVLLNQSDRTLSLVIPISGASQASAVETNETKNMEPAD
VTVTKESVSLPISGKSIVSVRIGF

Enzyme Prediction     

No EC number prediction in MGYG000001920_01589.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH30	129	401	4.7e-81	0.7280701754385965

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG5520	XynC	8.20e-47	138	419	143	404	O-Glycosyl hydrolase [Cell wall/membrane/envelope biogenesis].
pfam17189	Glyco_hydro_30C	8.79e-05	355	406	1	52	Glycosyl hydrolase family 30 beta sandwich domain.
cd14948	BACON	1.75e-04	41	127	7	83	Bacteroidetes-Associated Carbohydrate-binding (putative) Often N-terminal (BACON) domain. The BACON domain is found in diverse domain architectures and accociated with a wide variety of domains, including carbohydrate-active enzymes and proteases. It was named for its suggested function of carbohydrate binding; the latter was inferred from domain architectures, sequence conservation, and phyletic distribution. However, recent experimental data suggest that its primary function in Bacteroides ovatus endo-xyloglucanase BoGH5A is to distance the catalytic module from the cell surface and confer additional mobility to the catalytic domain for attack of the polysaccharide. No evidence for a direct role in carbohydrate binding could be found in that case. The large majority of BACON domains are found in Bacteroidetes.
pfam02055	Glyco_hydro_30	8.04e-04	142	238	127	237	Glycosyl hydrolase family 30 TIM-barrel domain.
pfam13004	BACON	0.004	76	127	14	61	Putative binding domain, N-terminal. The BACON (Bacteroidetes-Associated Carbohydrate-binding Often N-terminal) domain is an all-beta domain found in diverse architectures, principally in combination with carbohydrate-active enzymes and proteases. These architectures suggest a carbohydrate-binding function which is also supported by the nature of BACON's few conserved amino-acids. The phyletic distribution of BACON and other data tentatively suggest that it may frequently function to bind mucin. Further work with the characterized structure of a member of glycoside hydrolase family 5 enzyme, Structure 3ZMR, has found no evidence for carbohydrate-binding for this domain.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QDH54065.1	7.33e-172	1	444	1	547
QUT78601.1	1.00e-171	1	444	1	547
EDO10799.1	1.42e-171	1	444	1	547
QRQ55177.1	1.42e-171	1	444	1	547
ALJ48333.1	1.42e-171	1	444	1	547

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4QAW_A	5.30e-37	138	437	104	383	Structureof modular Xyn30D from Paenibacillus barcinonensis [Paenibacillus barcinonensis],4QAW_B Structure of modular Xyn30D from Paenibacillus barcinonensis [Paenibacillus barcinonensis],4QAW_C Structure of modular Xyn30D from Paenibacillus barcinonensis [Paenibacillus barcinonensis],4QAW_D Structure of modular Xyn30D from Paenibacillus barcinonensis [Paenibacillus barcinonensis],4QAW_E Structure of modular Xyn30D from Paenibacillus barcinonensis [Paenibacillus barcinonensis],4QAW_F Structure of modular Xyn30D from Paenibacillus barcinonensis [Paenibacillus barcinonensis],4QAW_G Structure of modular Xyn30D from Paenibacillus barcinonensis [Paenibacillus barcinonensis],4QAW_H Structure of modular Xyn30D from Paenibacillus barcinonensis [Paenibacillus barcinonensis]
4UQA_A	2.14e-36	138	437	125	405	ChainA, Carbohydrate Binding Family 6 [Acetivibrio thermocellus]
3GTN_A	2.56e-36	138	418	106	364	CrystalStructure of XynC from Bacillus subtilis 168 [Bacillus subtilis],3GTN_B Crystal Structure of XynC from Bacillus subtilis 168 [Bacillus subtilis],3KL0_A Crystal structure of the glucuronoxylan xylanohydrolase XynC from Bacillus subtilis [Bacillus subtilis subsp. subtilis str. 168],3KL0_B Crystal structure of the glucuronoxylan xylanohydrolase XynC from Bacillus subtilis [Bacillus subtilis subsp. subtilis str. 168],3KL0_C Crystal structure of the glucuronoxylan xylanohydrolase XynC from Bacillus subtilis [Bacillus subtilis subsp. subtilis str. 168],3KL0_D Crystal structure of the glucuronoxylan xylanohydrolase XynC from Bacillus subtilis [Bacillus subtilis subsp. subtilis str. 168],3KL3_A Crystal structure of Ligand bound XynC [Bacillus subtilis subsp. subtilis str. 168],3KL3_B Crystal structure of Ligand bound XynC [Bacillus subtilis subsp. subtilis str. 168],3KL3_C Crystal structure of Ligand bound XynC [Bacillus subtilis subsp. subtilis str. 168],3KL3_D Crystal structure of Ligand bound XynC [Bacillus subtilis subsp. subtilis str. 168],3KL5_A Structure Analysis of a Xylanase From Glycosyl Hydrolase Family Thirty: Carbohydrate Ligand Complexes Reveal this Family of Enzymes Unique Mechanism of Substrate Specificity and Recognition [Bacillus subtilis],3KL5_B Structure Analysis of a Xylanase From Glycosyl Hydrolase Family Thirty: Carbohydrate Ligand Complexes Reveal this Family of Enzymes Unique Mechanism of Substrate Specificity and Recognition [Bacillus subtilis],3KL5_C Structure Analysis of a Xylanase From Glycosyl Hydrolase Family Thirty: Carbohydrate Ligand Complexes Reveal this Family of Enzymes Unique Mechanism of Substrate Specificity and Recognition [Bacillus subtilis],3KL5_D Structure Analysis of a Xylanase From Glycosyl Hydrolase Family Thirty: Carbohydrate Ligand Complexes Reveal this Family of Enzymes Unique Mechanism of Substrate Specificity and Recognition [Bacillus subtilis]
4CKQ_A	1.07e-35	138	437	125	405	ChainA, Carbohydrate Binding Family 6 [Acetivibrio thermocellus],4UQ9_A Chain A, Carbohydrate Binding Family 6 [Acetivibrio thermocellus],4UQB_A Chain A, Carbohydrate Binding Family 6 [Acetivibrio thermocellus],4UQC_A Chain A, Carbohydrate Binding Family 6 [Acetivibrio thermocellus],4UQD_A Chain A, Carbohydrate Binding Family 6 [Acetivibrio thermocellus],4UQE_A Chain A, Carbohydrate Binding Family 6 [Acetivibrio thermocellus]
1NOF_A	3.41e-35	138	417	101	355	ChainA, xylanase [Dickeya chrysanthemi],2Y24_A Chain A, XYLANASE [Dickeya chrysanthemi]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q45070	2.02e-35	138	418	137	395	Glucuronoxylanase XynC OS=Bacillus subtilis (strain 168) OX=224308 GN=xynC PE=1 SV=1
Q6YK37	7.05e-34	138	424	138	403	Glucuronoxylanase XynC OS=Bacillus subtilis OX=1423 GN=xynC PE=3 SV=2

SignalP and Lipop Annotations

This protein is predicted as LIPO

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000001	0.000304	0.999717	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001920_01589.