CAZyme Information: MGYG000000675_00309

Basic Information

• Species: Bacteroides congonensis
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides congonensis
• CAZyme ID: MGYG000000675_00309
• CAZy Family: PL1
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
797	MGYG000000675_3|CGC4	87675.85	4.5216

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000675	5782172	MAG	Kazakhstan	Asia

• Gene Location: Start: 110953; End: 113346 Strand: +

Full Sequence      

MRYFLFILLAGLFSACSADDDSNAAATAAKLEVSKNEVKLSNVNGSFTINITATSEWTAE
VTSTGGWLSISKNSGEGNGDLRLFFTENTDGPKRTGTVKVSMTGAGSTLEQEISVEQLGA
DPDILFDCSSDPLPFREGTFVCKVVANVEWDVDIAEEYNWIKLKETTPRTRSFATDEVTF
TVDANANQEDRTAILAFNSVGDYTLQRILKVTQDGVSGKVTIEQDEYILPYKFRTLVISA
PQGENPVDYDASISETWITQDKRNSTTDEVVLNIEDNSNSPLPRTATVKILDKTLTIFQY
GRPDTSIGDDTSTSILAFPGAEGGGRFTTGGRGGEIYHVTTLADYNQNETPVEGSLRYGV
EKSNQPRTIVFDVSGVIELKRGLYLNEFPNLSIIGQTAPGDGITLKNYNFTFNLAKDPAK
GAGSSLNAIVRFLRCRPGDQHADYGEDAIGGRYFKDAIIDHVTASWSVDETLTFYGVQNF
TAQWCIASESLNLSNHAKGAHGYGAMFSGDNASFHHILLAHHGSRCPRISDLSAPGTQES
FDFTGYFDVRNNVYYNWSGRGQGSYGGKYATFNLTNCYYKPGPATGTNNRSYRVLSSDPT
ARAYINGNYVAGSSDVTADNWTRGIWEQFDSSLGTVPEAEKQAMKMADYQPYSKVTNHTA
IQAYDKVLEYAGASLRRDVIDQRVIREVKEGTYTYIGSKPEEDGKDKQLGLIDTVADTEG
YVPVKSLTLWPDTDGDGIPDIWEEAYGLNPNDPSDAWQINSSVDPNGRYPNIEVYFHNLV
QHIIYYQNQGGVVMEKK

Enzyme Prediction     

No EC number prediction in MGYG000000675_00309.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
PL1	374	579	9.4e-66	0.994535519125683

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd14948	BACON	2.55e-16	31	117	2	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	2.01e-06	138	214	16	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.
pfam19190	BACON_2	3.93e-06	46	109	21	84	Viral BACON domain. This family represents a distinct class of BACON domains found in crAss-like phages, the most common viral family in the human gut, in which they are found in tail fiber genes. This suggests they may play a role in phage-host interactions.
pfam13004	BACON	2.77e-05	150	213	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.
pfam13004	BACON	1.00e-04	57	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
QIU94510.1	0.0	1	797	1	797
QDH54496.1	0.0	1	797	1	795
QNL41094.1	0.0	1	797	1	795
QGT73513.1	0.0	1	797	1	795
QUT78065.1	0.0	1	797	1	795

PDB Hits     

has no PDB hit.

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
B8NQQ7	2.44e-41	312	780	17	414	Probable pectate lyase C OS=Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167) OX=332952 GN=plyC PE=3 SV=1
B0XMA2	1.35e-39	313	780	19	415	Probable pectate lyase C OS=Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) OX=451804 GN=plyC PE=3 SV=1
Q4WL88	3.39e-39	313	780	19	415	Probable pectate lyase C OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=plyC PE=3 SV=1
Q2UB83	4.51e-39	312	780	17	414	Probable pectate lyase C OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=plyC PE=3 SV=1
Q0CLG7	8.32e-39	313	780	18	414	Probable pectate lyase C OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=plyC PE=3 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
0.000174	0.165339	0.834255	0.000093	0.000078	0.000064

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000675_00309.