CAZyme Information: MGYG000002935_00098

Basic Information

• Species: Phocaeicola sp002161765
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Phocaeicola; Phocaeicola sp002161765
• CAZyme ID: MGYG000002935_00098
• CAZy Family: GH5
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
593	MGYG000002935_1|CGC2	64352.73	4.1469

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002935	2727252	MAG	Finland	Europe

• Gene Location: Start: 123161; End: 124942 Strand: -

Full Sequence      

MKYIRNYLVLFLTFVTGTAMFASCSDDEEGGFSGETKISATELAFAKSGGTQTLSIASGT
EPQVTSNQDWCNVAFVNVTQRGTYTYDITAEANTETEDRTATLSVTAGSFSASVQVTQTA
GDGLIVAQNSYEMPSAGGSLEVTLTTNGDYSYTINDSWITEAEMSDARAMSEYTLHFTVS
ANHGAERIGTITFTLNDLSETVSIVQEAGQGGQGVSGETPYEIAASLGLGWNLGNQLDAH
NNGVAEEGWGNEPTTQALFDRVAAAGFTSVRIPVTWLGKVGAAPDYTIDADYLNRVAEVV
GYAENAGLNAIINIHHDGADSQYWLNIKNAAADETVNEAVKAQLKAMWTQIAERFRDKGN
FLVFEAMNEIHDGGWGWGDNRTDGGKQYAVLNEWNQVFVDAVRATGGNNTERYLGVPGYV
TNIDLTVENFVLPTDAVQNRLMVAVHFYDPNEFVLEATASEWGHTGDPAKKATWGDEDNV
RTQFGKMKSAFIDKGIPAYIGEMGCVHRNDARAESFRLYYLEYVCKAAKDYGLPPFYWDN
GSSGSGAETSGLFNHATGEMLNNAEEVIDVMKRGIFTEDESYTLQSVYDGAPQ

Enzyme Prediction     

EC	3.2.1.4

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH5	246	541	1.2e-97	0.9891304347826086

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam00150	Cellulase	2.70e-56	237	544	1	272	Cellulase (glycosyl hydrolase family 5).
COG2730	BglC	5.59e-25	217	551	41	370	Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism].
cd14948	BACON	2.10e-16	124	207	2	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.
cd14948	BACON	4.24e-16	37	118	3	82	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.
pfam13004	BACON	1.70e-08	60	118	1	60	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
ADY35478.1	0.0	5	593	2	592
QUT88430.1	5.12e-258	1	593	1	598
ALJ60576.1	1.80e-222	126	593	41	512
QRX62664.1	1.15e-183	129	593	43	513
AVM57519.1	4.69e-180	129	593	88	563

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6WQY_A	1.65e-221	213	577	17	384	ChainA, Cellulase [Phocaeicola salanitronis DSM 18170]
4YHE_A	7.00e-130	222	593	9	386	NativeBacteroidetes-affiliated Gh5 Cellulase Linked With A Polysaccharide Utilization Locus [Bacteroidetes bacterium AC2a],4YHE_B Native Bacteroidetes-affiliated Gh5 Cellulase Linked With A Polysaccharide Utilization Locus [Bacteroidetes bacterium AC2a]
4YHG_A	5.60e-129	222	593	9	386	NativeBacteroidetes-affiliated Gh5 Cellulase Linked With A Polysaccharide Utilization Locus [Bacteroidetes bacterium AC2a],4YHG_B Native Bacteroidetes-affiliated Gh5 Cellulase Linked With A Polysaccharide Utilization Locus [Bacteroidetes bacterium AC2a]
2JEP_A	7.70e-86	222	575	37	394	Nativefamily 5 xyloglucanase from Paenibacillus pabuli [Paenibacillus pabuli],2JEP_B Native family 5 xyloglucanase from Paenibacillus pabuli [Paenibacillus pabuli],2JEQ_A Family 5 xyloglucanase from Paenibacillus pabuli in complex with ligand [Paenibacillus pabuli]
3NDY_A	2.01e-65	214	575	6	341	Thestructure of the catalytic and carbohydrate binding domain of endoglucanase D from Clostridium cellulovorans [Clostridium cellulovorans],3NDY_B The structure of the catalytic and carbohydrate binding domain of endoglucanase D from Clostridium cellulovorans [Clostridium cellulovorans],3NDY_C The structure of the catalytic and carbohydrate binding domain of endoglucanase D from Clostridium cellulovorans [Clostridium cellulovorans],3NDY_D The structure of the catalytic and carbohydrate binding domain of endoglucanase D from Clostridium cellulovorans [Clostridium cellulovorans],3NDZ_A The structure of the catalytic and carbohydrate binding domain of endoglucanase D from Clostridium cellulovorans bound to cellotriose [Clostridium cellulovorans],3NDZ_B The structure of the catalytic and carbohydrate binding domain of endoglucanase D from Clostridium cellulovorans bound to cellotriose [Clostridium cellulovorans],3NDZ_C The structure of the catalytic and carbohydrate binding domain of endoglucanase D from Clostridium cellulovorans bound to cellotriose [Clostridium cellulovorans],3NDZ_D The structure of the catalytic and carbohydrate binding domain of endoglucanase D from Clostridium cellulovorans bound to cellotriose [Clostridium cellulovorans]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O08342	8.81e-82	219	575	39	399	Endoglucanase A OS=Paenibacillus barcinonensis OX=198119 GN=celA PE=1 SV=1
P28623	5.99e-64	214	575	37	372	Endoglucanase D OS=Clostridium cellulovorans (strain ATCC 35296 / DSM 3052 / OCM 3 / 743B) OX=573061 GN=engD PE=1 SV=2
P28621	3.87e-63	214	554	36	355	Endoglucanase B OS=Clostridium cellulovorans (strain ATCC 35296 / DSM 3052 / OCM 3 / 743B) OX=573061 GN=engB PE=3 SV=1
Q12647	1.84e-55	201	557	6	347	Endoglucanase B OS=Neocallimastix patriciarum OX=4758 GN=CELB PE=2 SV=1
A7LXT7	9.17e-55	18	572	27	499	Xyloglucan-specific endo-beta-1,4-glucanase BoGH5A OS=Bacteroides ovatus (strain ATCC 8483 / DSM 1896 / JCM 5824 / BCRC 10623 / CCUG 4943 / NCTC 11153) OX=411476 GN=BACOVA_02653 PE=1 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
0.000000	0.000002	1.000059	0.000000	0.000000	0.000000

TMHMM  Annotations     

start	end
7	24