CAZyme Information: MGYG000001789_02877

Basic Information

• Species: Phocaeicola sp002161565
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Phocaeicola; Phocaeicola sp002161565
• CAZyme ID: MGYG000001789_02877
• CAZy Family: GH30
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
536		59783.84	4.3471

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001789	3544186	MAG	Denmark	Europe

• Gene Location: Start: 193; End: 1803 Strand: +

Full Sequence      

MKQLKSFLFLFLASTLFWACSDDDTVNKSLWGDSYARFVRNAMTVTSTEGTAEAIIDWQQ
STWEITLGEGNIVTNVTPTSGGDNNGEHQFTKVTLTCNANTSMDTRTQVIRLTDRNGTTT
ELTITQEGAGGIVLTVDPAVKYQPVAGFGGMYAVSIWGTPTITADEMNKMYSPDGLGYSI
LRLMIYADETRWADDVDGAKIAQSHGATVFACPWNIPAEWADKADDKDHLKPEHYTAYAD
HLIKYINFMKQNGVDIYAVSVQNEPDMDFTAWTPQEVVNFLKQEGARIRETGVKLMSPEA
CGYQPEYTDAVLNDAEAFAQTDIVAGHLYQGFIDLSSDYVKGRHDYVCGLYPRLGGKTWW
MTEHLFNDGEKEEDPSMWQFLNWDYNFSHLAKEIHMCMDGYCSAYLYWYLKRFYGMIGDN
NPRSPVAEGEIAKNGYILAHYAQYATNTTRIAVTSGSENIDATAYINETGNEITLVLLNQ
SDRTLSIQIPMDGISQATAVETSETKNMETIDVNVTGEFVSLSISGESIVSVRIKL

Enzyme Prediction     

No EC number prediction in MGYG000001789_02877.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH30	135	492	1.6e-109	0.9766081871345029

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG5520	XynC	8.76e-60	129	529	31	423	O-Glycosyl hydrolase [Cell wall/membrane/envelope biogenesis].
pfam02055	Glyco_hydro_30	3.39e-06	145	330	1	237	Glycosyl hydrolase family 30 TIM-barrel domain.
cd14948	BACON	3.79e-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.
pfam17189	Glyco_hydro_30C	6.59e-04	449	498	3	52	Glycosyl hydrolase family 30 beta sandwich domain.
pfam13004	BACON	7.81e-04	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
ALJ58222.1	1.59e-236	1	536	1	546
QUT90760.1	3.20e-236	1	536	1	546
EDO10799.1	9.72e-231	1	534	1	545
QRQ55177.1	9.72e-231	1	534	1	545
ALJ48333.1	9.72e-231	1	534	1	545

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3GTN_A	4.40e-51	134	482	5	334	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]
1NOF_A	1.52e-49	136	509	5	355	ChainA, xylanase [Dickeya chrysanthemi],2Y24_A Chain A, XYLANASE [Dickeya chrysanthemi]
4QAW_A	1.99e-48	136	529	6	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	5.34e-48	135	529	25	405	ChainA, Carbohydrate Binding Family 6 [Acetivibrio thermocellus]
4CKQ_A	2.75e-47	135	529	25	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q45070	3.90e-50	134	482	36	365	Glucuronoxylanase XynC OS=Bacillus subtilis (strain 168) OX=224308 GN=xynC PE=1 SV=1
Q6YK37	2.87e-48	136	535	39	422	Glucuronoxylanase XynC OS=Bacillus subtilis OX=1423 GN=xynC PE=3 SV=2
P17439	1.45e-07	131	333	83	335	Lysosomal acid glucosylceramidase OS=Mus musculus OX=10090 GN=Gba PE=1 SV=1
O16580	3.37e-07	127	344	80	349	Putative glucosylceramidase 1 OS=Caenorhabditis elegans OX=6239 GN=gba-1 PE=1 SV=2
Q70KH2	4.53e-07	131	493	103	517	Lysosomal acid glucosylceramidase OS=Sus scrofa OX=9823 GN=GBA PE=3 SV=1

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 MGYG000001789_02877.