CAZyme Information: MGYG000000348_00918

Basic Information

• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; CAG-485
• CAZyme ID: MGYG000000348_00918
• CAZy Family: GH5
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
576	MGYG000000348_12|CGC1	63189.74	4.6005

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000348	2655711	MAG	Sweden	Europe

• Gene Location: Start: 60654; End: 62384 Strand: -

Full Sequence      

MKKILFLATLISLVLGLGSCSDSDKTPDGPFAGEFKVGVTELTFLKTAATQTLYVAAPSK
PAVTSDAEWLTVGDIALNGESNSVYAVAVNVTDNNVYDNRTGNLKITCGANEATVKVTQR
NSDGILLADGYAAPEVKADGETLEIPVLATGEYTATVSDTWMEIVPAPVRGLVESKVYVK
VAANYRAEAREGSVTIALDSDDTQSVTVAIKQAATASTGQCDETAFQTAANISMAINIGN
TLEAIGGETAWGAAKINADYIRSIREAGFDAVRLPVAWYNHSDKNTLKIDESWMNRVDEV
VRLCIANGLYVFMNIHWDEGWMELNIDSYSPDVDRIQRELWTQIADRFKDYDKHLVFCGA
NEAGQDTQASADALKAYMQTFIDVVRASGSNNANRVLVVQSPGTDIDRAVKYCAGNLPKD
KVADRMMLEVHCYDPSDFTIMQNDGEWGANSKVRYFWGQDYHTGTDRDCTWGEENHIDTQ
MQKLKANFVDKGIPVIIGEFSCGRRRSFVASIDEDRHRASRCYYHSYIVKSAKTNGAVPF
LWDTPNEMFNRQTGAVIDPDNLAAIQQGAANGKYPY

Enzyme Prediction     

No EC number prediction in MGYG000000348_00918.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH5	248	544	1.2e-90	0.9855072463768116

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam00150	Cellulase	1.97e-46	242	543	10	267	Cellulase (glycosyl hydrolase family 5).
COG2730	BglC	9.67e-16	237	501	56	322	Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism].
cd14948	BACON	9.26e-13	34	119	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.
cd14948	BACON	5.21e-12	135	213	10	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.
pfam13004	BACON	1.24e-07	62	119	4	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
QCD42340.1	1.66e-139	3	576	13	593
SCD22090.1	9.75e-119	11	576	11	566
SCM57160.1	1.53e-117	11	576	11	566
QQA29804.1	9.98e-113	17	576	24	593
QUT37093.1	9.98e-113	17	576	24	593

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5OYC_A	8.11e-99	213	569	34	393	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	6.37e-98	213	569	34	393	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	2.91e-72	237	576	15	378	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	6.86e-69	127	568	10	465	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]
6WQY_A	6.25e-50	223	558	22	369	ChainA, Cellulase [Phocaeicola salanitronis DSM 18170]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
A7LXT7	7.27e-68	127	568	45	500	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	2.36e-45	224	568	39	398	Endoglucanase A OS=Paenibacillus barcinonensis OX=198119 GN=celA PE=1 SV=1
P23660	6.15e-40	222	549	24	340	Endoglucanase A OS=Ruminococcus albus OX=1264 GN=celA PE=1 SV=1
P28623	6.13e-38	215	562	33	357	Endoglucanase D OS=Clostridium cellulovorans (strain ATCC 35296 / DSM 3052 / OCM 3 / 743B) OX=573061 GN=engD PE=1 SV=2
P10477	9.83e-38	219	569	51	385	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

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	0.000011	1.000051	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000348_00918.