CAZyme Information: MGYG000001306_01749

Basic Information

• Species: Phocaeicola coprocola
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Phocaeicola; Phocaeicola coprocola
• CAZyme ID: MGYG000001306_01749
• CAZy Family: GH5
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
567	MGYG000001306_33|CGC2	64071.52	4.2219

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001306	4295617	Isolate	not provided	not provided

• Gene Location: Start: 88803; End: 90506 Strand: -

Full Sequence      

MKNTFIYFLGTLTCLMSLLLSACSEDDATGAPYLKISKEELVFGKHEGEALLYIQSNAAY
EVTSDAADWCSVVQQVSTSEKTAKYLVHVTENPNTENRTAVITVKGAEVNGTVKVVQTAN
DYLLVEEHEYTLPGEGGEFTVQMQTTGDCQIDINADWIQHVDTRAVETRTETFMVAQNAT
GEIRTATIVFTLDNLTESVTVTQEALSVPEADKTGMEQDAPELMKNIKIGWNLGNSLEAT
GGETAWGNPATTLAMIDKIREMGFNAVRIPCAWDQYLSDETTYEIKSSWLSRVKEVVDYC
MQNDLYAILNIHWDGGWLENDIPNGYSEEVNNKQKVLWTQIATYFRDYDEHLLFAGCNEP
NVEDEDDMATLLKYEQTFVDAVRATGGKNVYRNLIVQGPSTDIDKTMQYMTSLPVDMTPD
RLSVEVHYYSSWQFCGMENDESWGKAFYFWGEENKKYATGTYEGRWDNICGEDYIKSQFQ
KLKEKFTDQGVPVIIGEFAAVRRTLPDQQAQEGHDLSRAAFDKCVVREANARGLVPFYWD
RGDGVFDRKNLQVYDELEYNGLMEGIK

Enzyme Prediction     

EC	3.2.1.4

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH5	243	542	1.8e-97	0.9891304347826086

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam00150	Cellulase	2.53e-56	237	540	10	267	Cellulase (glycosyl hydrolase family 5).
COG2730	BglC	2.61e-21	230	540	54	358	Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism].
cd14948	BACON	2.99e-16	122	204	1	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	1.79e-15	33	117	1	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	1.05e-09	59	117	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
QRM99680.1	1.32e-282	14	566	14	566
SCD22090.1	5.74e-175	7	567	7	560
SCM57160.1	1.31e-173	21	567	22	560
QPH58994.1	8.12e-172	16	567	19	569
QBJ18684.1	3.26e-171	16	567	19	569

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5OYC_A	6.51e-123	212	565	37	392	GH5endo-xyloglucanase from Cellvibrio japonicus [Cellvibrio japonicus Ueda107],5OYC_B GH5 endo-xyloglucanase from Cellvibrio japonicus [Cellvibrio japonicus Ueda107],5OYD_A GH5 endo-xyloglucanase from Cellvibrio japonicus [Cellvibrio japonicus Ueda107],5OYD_B GH5 endo-xyloglucanase from Cellvibrio japonicus [Cellvibrio japonicus Ueda107],5OYE_A GH5 endo-xyloglucanase from Cellvibrio japonicus [Cellvibrio japonicus Ueda107],5OYE_B GH5 endo-xyloglucanase from Cellvibrio japonicus [Cellvibrio japonicus Ueda107]
6HA9_A	5.20e-122	212	565	37	392	Structureof an endo-Xyloglucanase from Cellvibrio japonicus complexed with XXXG(2F)-beta-DNP [Cellvibrio japonicus Ueda107],6HA9_B Structure of an endo-Xyloglucanase from Cellvibrio japonicus complexed with XXXG(2F)-beta-DNP [Cellvibrio japonicus Ueda107],6HAA_A Structure of a covalent complex of endo-Xyloglucanase from Cellvibrio japonicus after reacting with XXXG(2F)-beta-DNP [Cellvibrio japonicus Ueda107],6HAA_B Structure of a covalent complex of endo-Xyloglucanase from Cellvibrio japonicus after reacting with XXXG(2F)-beta-DNP [Cellvibrio japonicus Ueda107]
4W8A_A	7.56e-87	218	567	1	368	Crystalstructure of XEG5B, a GH5 xyloglucan-specific beta-1,4-glucanase from ruminal metagenomic library, in the native form [uncultured bacterium],4W8B_A Crystal structure of XEG5B, a GH5 xyloglucan-specific beta-1,4-glucanase from ruminal metagenomic library, in complex with XXLG [uncultured bacterium]
3ZMR_A	5.04e-71	108	566	3	466	Bacteroidesovatus GH5 xyloglucanase in complex with a XXXG heptasaccharide [Bacteroides ovatus],3ZMR_B Bacteroides ovatus GH5 xyloglucanase in complex with a XXXG heptasaccharide [Bacteroides ovatus]
2JEP_A	7.63e-68	219	567	34	395	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
A7LXT7	5.40e-70	108	566	38	501	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
O08342	4.58e-61	220	567	40	400	Endoglucanase A OS=Paenibacillus barcinonensis OX=198119 GN=celA PE=1 SV=1
P28621	7.03e-58	213	551	34	359	Endoglucanase B OS=Clostridium cellulovorans (strain ATCC 35296 / DSM 3052 / OCM 3 / 743B) OX=573061 GN=engB PE=3 SV=1
P10477	2.00e-53	220	565	57	384	Cellulase/esterase CelE OS=Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) OX=203119 GN=celE PE=1 SV=2
P28623	1.89e-52	220	551	43	357	Endoglucanase D OS=Clostridium cellulovorans (strain ATCC 35296 / DSM 3052 / OCM 3 / 743B) OX=573061 GN=engD PE=1 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
0.000000	0.000000	1.000043	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001306_01749.