CAZyme Information: MGYG000001275_00172

Basic Information

• Species: CAG-485 sp900321585
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; CAG-485; CAG-485 sp900321585
• CAZyme ID: MGYG000001275_00172
• CAZy Family: GH5
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
576	MGYG000001275_2|CGC1	63301.8	4.6055

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001275	2994513	MAG	Italy	Europe

• Gene Location: Start: 34713; End: 36443 Strand: -

Full Sequence      

MKKILFFATLISLVLGLGSCSDSDKTPDGPFAGEFKVGVTELTFLKTAATQTLYVAAPSK
PAVTSDSEWLSVGDIALNGESNSVYAVPVNVTDNNVYDNRTGNLKITCGANEATVKVTQR
NSDGILLADGYTAPEVKADGETLEIPILATGDYTATVSDTWMEIVPAPVRGLTESKIYVK
VAANYRPESREGSVVITLNSDNATNLTVAVRQGASASSGMCDETAFETASSISMAVNIGN
TLEAIGGETAWGAAKINADYIRSIRESGFDAVRLPVAWYNHSDKNTLKIDEDWMKRVDEV
VQLCIANGLYVFMNIHWDEGWMELNIDSYSADVDRIQRELWTQIADRFKDYDKHLVFCGA
NEAGKDTQASADALKAYMQTFIDVVRASGSNNANRVLVVQAPGTDIDRAVKYCTGNMPTD
NVADRMMLEVHCYDPSDFTLLQNDGEWGADSKVRYFWGQDFHTGTDRDCTWGEENHIDTQ
MQKLKTNFVDKGIPVIIGEFGCGRRRTFLATIDEARHRASRCYYHSHIVKSAKNHGAVPF
LWDTPNELFNRQTGAVIDPDNLTAMQQGAADGKYPY

Enzyme Prediction     

No EC number prediction in MGYG000001275_00172.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH5	248	544	5.9e-91	0.9855072463768116

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam00150	Cellulase	1.37e-47	242	543	10	267	Cellulase (glycosyl hydrolase family 5).
COG2730	BglC	5.02e-18	236	501	55	322	Aryl-phospho-beta-D-glucosidase BglC, GH1 family [Carbohydrate transport and metabolism].
cd14948	BACON	7.40e-12	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	4.54e-11	135	212	10	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	3.80e-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	5.27e-138	3	576	13	593
SCD22090.1	2.02e-124	11	576	11	566
SCM57160.1	8.01e-124	11	576	11	566
QQA29804.1	3.39e-110	17	576	24	593
QUT65987.1	6.73e-110	17	576	24	593

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5OYC_A	3.21e-98	217	569	38	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	2.52e-97	217	569	38	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	6.50e-70	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	1.04e-66	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]
2JEP_A	2.09e-48	237	568	47	393	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	1.09e-65	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	2.29e-44	237	568	52	398	Endoglucanase A OS=Paenibacillus barcinonensis OX=198119 GN=celA PE=1 SV=1
P10477	9.15e-39	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
P28623	3.28e-38	213	563	31	358	Endoglucanase D OS=Clostridium cellulovorans (strain ATCC 35296 / DSM 3052 / OCM 3 / 743B) OX=573061 GN=engD PE=1 SV=2
P23660	1.43e-37	222	549	24	340	Endoglucanase A OS=Ruminococcus albus OX=1264 GN=celA 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	0.000009	1.000044	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001275_00172.