CAZyme Information: MGYG000002209_00364

Basic Information

• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; CAG-462
• CAZyme ID: MGYG000002209_00364
• CAZy Family: PL10
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
614		69619.82	6.2217

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002209	3647221	MAG	Spain	Europe

• Gene Location: Start: 76375; End: 78219 Strand: +

Full Sequence      

MKIMNLSFKVGLLLWALSISACSEEDKELQETLTVSKTVLNISEEGSSESISINSSHKWS
IVCEEYWVKCSLTSGSGNKNVTLTVSPNKNKEERQTKVVVKGINKEVIVHIIQAGIVPTI
QISLTQKTLDSSGEEFTVGVTAEGLQWTAEVPASAQSWISLKEKSDKQVSFVAKLNNNGK
ERTANLIFREIGKTDSKTVKVTQGIFKSTVADIAWSKLLSKVSDSWYETNEAKEVADNVL
LYQRDCGGWHKNIEMHHLLTDTEKEKVTAEKKEKGCFDNGATTMEMRFLAKMYKHVPDSR
YRDAFAKGLNYIMNAQYSTGGWPQYFPLRGGYSDFITFNDDLMVNLLKLLRDVYESGENF
AAIVEDETKRKAKETFEKGLDCILNCQIVDEGAKTLWCAQHDPVTMDPAVGRPHELPSFS
GCEGARILEFLMTIENPSDKVKEAVVAAAEWLENHKIPNKKVVDVKDASGNTIDRKVEDC
AGEDMWGRFIQLGGEVAERVYTNLFNEFLKDGKRTYSSADGKSITYYYKDNAVKSYDSRK
AYQPIYGIYDNNYAFLFYRFLYNYEDTEPIKDEHGVMVDTSLRAENRRSYQYVGNWPQRI
LREKYPAWKAKQGM

Enzyme Prediction     

No EC number prediction in MGYG000002209_00364.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
PL10	243	495	9.6e-93	0.8715277777777778

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam09492	Pec_lyase	6.59e-94	243	493	1	250	Pectic acid lyase. Members of this family are isozymes of pectate lyase (EC:4.2.2.2), also called polygalacturonic transeliminase and alpha-1,4-D-endopolygalacturonic acid lyase.
TIGR02474	pec_lyase	1.86e-86	243	494	1	252	pectate lyase, PelA/Pel-15E family. Members of this family are isozymes of pectate lyase (EC 4.2.2.2), also called polygalacturonic transeliminase and alpha-1,4-D-endopolygalacturonic acid lyase. [Energy metabolism, Biosynthesis and degradation of polysaccharides]
cd14948	BACON	1.55e-11	119	203	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	3.74e-11	59	114	28	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	3.89e-04	59	114	3	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
QQR09858.1	7.08e-123	211	611	29	442
ANU62800.2	7.08e-123	211	611	29	442
ASB36702.1	7.08e-123	211	611	29	442
AAW84062.1	5.42e-78	201	520	15	328
QEC53563.1	1.73e-77	212	492	37	319

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1R76_A	5.85e-44	225	494	76	360	ChainA, pectate lyase [Niveispirillum irakense]
1GXM_A	4.73e-42	236	492	37	283	Family10 polysaccharide lyase from Cellvibrio cellulosa [Cellvibrio japonicus],1GXM_B Family 10 polysaccharide lyase from Cellvibrio cellulosa [Cellvibrio japonicus],1GXN_A Family 10 polysaccharide lyase from Cellvibrio cellulosa [Cellvibrio japonicus]
1GXO_A	6.18e-41	236	492	37	283	MutantD189A of Family 10 polysaccharide lyase from Cellvibrio cellulosa in complex with trigalaturonic acid [Cellvibrio japonicus]

Swiss-Prot Hits     

has no Swissprot hit.

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
0.000241	0.120004	0.879572	0.000067	0.000068	0.000055

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002209_00364.