CAZyme Information: MGYG000000765_00758

Basic Information

• Species: Porphyromonas_A bennonis
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae; Porphyromonas_A; Porphyromonas_A bennonis
• CAZyme ID: MGYG000000765_00758
• CAZy Family: CBM32
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
932	MGYG000000765_8|CGC1	103142.96	6.6952

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000765	2007181	MAG	Bangladesh	Asia

• Gene Location: Start: 40571; End: 43369 Strand: +

Full Sequence      

MNNSHKITFLSLSLLILVLCGCKRDPSQEAAYIDIGEGNEILFSAELGTKDIGVKTNVST
LTAKASESWLSARVGRGSITISVTANTDKAPRTGKILVSGEGASATISVRQEGLEPSILV
SPETSTVTADAQSLSLTVQANVDYLLPDLSETPWITLTSKDQSKKPHQIILSIAANATMA
ERSATLAFRSKDVSPEIIREVVITQTAPTDYSGEGGSAIGADEKITVASGSTSSYQSGGE
IEKSFDGDMGTMYHSKWDNSSTSYFPITLEYHLAGAETVDYLVYHPRQTGNNGHFKEVEL
WVKKSDGDFKKQGDYDFKGTGEPKKVDFSPALEGVTAFRFVVKSGAGDGQGFASCAEMEF
YRRNKDNAVPTNIFTDGTASTLRPGVTEEQIRAISNPLYREIALFLYNGKYPSEFRIQDY
RAWPHPNDWIKKSKTNPQNLLDNATGIVAEAGKELIVLVGKTSGHSGLSIKVQNLDRPGG
DGYNDGSSTYPLSEGVNKIIPSNSGLIYVLYHTPSYKTAPKIRIHFATGNVNGYFDSEKH
SKEDWKRLLAGAKYKYFDVLGKEAHLTFPTEGFRKYAGEDGPELIAQYDELVTLETDLMG
LKKYDLPRVNRSYFHAMYGNYMYATWYRTAYNVSDENVLKVMCDKETFRKQPWGPAHETG
HNYQTRPGFMWAGMTEVTNNVHANYVNVKFGNTSRLSSENRYLSGYNTYHIDLSGLKSGW
TRPPYIRAGGIYDTVFEKLVPLWQLYLYFTEVKGQKDFYPDLYEKVRKNPNPPTDEKCLL
EFTRLASEISGYDLTDFFEAWSFYTPYKGVVEDYGKKNINLTSSLANEYRAKIVSMGLPK
PKEALQYITDKNIDLYRHPKPVVAGTYGRNGLKITVTGTTNAVAYEAVMDGRVIALSPDP
TFDLPVEAGSATSTLTVRAIAVDGTRTALTAK

Enzyme Prediction     

No EC number prediction in MGYG000000765_00758.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam13402	Peptidase_M60	4.79e-43	529	802	1	268	Peptidase M60, enhancin and enhancin-like. This family of peptidases contains a zinc metallopeptidase motif (HEXXHX(8,28)E) and possesses mucinase activity. It includes the viral enhancins as well as enhancin-like peptidases from bacterial species. Enhancins are a class of metalloproteases found in some baculoviruses that enhance viral infection by degrading the peritrophic membrane (PM) of the insect midgut. Bacterial enhancins are found to be cytotoxic when compared to viral enhancin, however, suggesting that the bacterial enhancins do not enhance infection in the same way as viral enhancin. Bacterial enhancins may have evolved a distinct biochemical function. These bacterial domains are peptidases targetting host glycoproteins and thus probably play an important role in successful colonisation of both vertebrate mucosal surfaces and the invertebrate digestive tract by both mutualistic and pathogenic microbes. This family has been augmented by a merge with the sequences in the Enhancin Pfam family.
cd14948	BACON	2.27e-14	39	112	7	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	1.19e-10	117	205	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.
pfam17291	M60-like_N	1.16e-07	445	525	23	107	N-terminal domain of M60-like peptidases. This accessory domain has a jelly roll topology.
pfam19190	BACON_2	5.40e-07	43	114	11	91	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QCT79445.1	3.95e-232	5	930	4	938
QRP89238.1	3.95e-232	5	930	4	938
QUU03487.1	9.95e-230	5	930	4	938
QRM71921.1	6.28e-228	9	924	10	922
QTO25368.1	6.28e-228	9	924	10	922

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7SCI_A	4.30e-71	373	850	14	487	ChainA, Peptidase M60 domain-containing protein [Akkermansia muciniphila ATCC BAA-835]
5KD2_A	6.85e-55	373	905	34	585	BT_4244metallopeptidase from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482]
5KD5_A	3.89e-51	408	905	23	537	BT_4244metallopeptidase from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482],5KD8_A BT_4244 metallopeptidase in complex with Tn antigen. [Bacteroides thetaiotaomicron VPI-5482]
7BLG_A	1.33e-43	222	363	22	162	ChainA, family 32 carbohydrate-binding module from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482],7BLH_AAAA Chain AAAA, family 32 carbohydrate-binding module from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482],7BLJ_A Chain A, family 32 carbohydrate-binding module from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482],7BLK_A Chain A, family 32 carbohydrate-binding module from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482]
5EV7_A	4.22e-34	485	880	78	439	Thecrystal structure of a functionally unknown conserved protein mutant from Bacillus anthracis str. Ames [Bacillus anthracis str. Ames]

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
0.000000	0.000000	1.000051	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000765_00758.