CAZyme Information: MGYG000001551_03099

Basic Information

• Species: Odoribacter massiliensis
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Marinifilaceae; Odoribacter; Odoribacter massiliensis
• CAZyme ID: MGYG000001551_03099
• CAZy Family: CBM32
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
918	MGYG000001551_11|CGC26	103911.36	4.7432

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001551	4400991	Isolate	not provided	not provided

• Gene Location: Start: 3404257; End: 3407013 Strand: -

Full Sequence      

MKQFLFIIFALALFACKDDKVDKEPYFEIKWTSDTVRFNTGGGNTVIPVSTNQDIELEYT
AEWFTATWNAKQNNIYITTETNKNSDPNTDQLIIHAGTFQKTLRIIQLGQTPALIPEQTS
YRVSEDTSTLYIPVTANVPFTTEITFEDNEEEEWLTSIERRDTLTNGNIRLAFHVTAYTA
LTPREAIITLNGEKNQNAVITVTQSALDSVYSPSDPEDIGSDLKITVNAGKASSFQPGEE
IERSFDGNTSTLYHSAYDNSKPNYFPIDLEYFFTDAEQIDYLIYYPRSDGSKNGPIKEFR
LYIKTEGDTDYKPYQGTFDFNGKGSPSRITFTEPLIHPRAIKFQVLSGDGDGNGFVSCAE
MEFYRKNPNNSITDIFTDASCSELKAGVTYEQICTMENEFYRNIAKYMFAGEYPKEFRIA
SYKPYPYPSQDEDLKTNTFTLLDNPTGISVKSGEELVVLVGDTHGSDLSVRVIDWNNGYG
SSSDYMLTEGANKLKMNKSGLVYLMYHNNGTQPVNVHFATGKVNGFFDATRHSDTDYRTL
INNAQDKHFDVLGKYTHMCFPVSKFRSACPEKGQRLVELYDSLVLLEHQLLGLYKYNRIQ
KNRISFVVDYEESTYMYATNFRTAYAPGTLDEILNPAKFRSTAIWGPAHEVGHVHQTGIG
MKWIGMTEVTNNIMSLHVQTTFGNRSRQIEDDRYATGFRTLLCHDYPFCTSDGDGGNDVF
VQLIPFWQLQLYNAKVLGKSGFYPDMYEQVRIDEAAITPTDGEAQINFVKMACQKSGYNL
LKFFERWGFLTPVDKTIDDYAQRQLTVTPEMIDRVKAEIEAMNLKTPLAIEYLRDDNIAL
YKNPQPVKTGTASLNGSTITLTGWSNIVAYEIYNTSTNGDRYLDQILLPSGQLKLNLIND
KTEVYAIAADGKQTAVSW

Enzyme Prediction     

No EC number prediction in MGYG000001551_03099.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam13402	Peptidase_M60	2.39e-43	521	788	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	8.93e-07	117	205	5	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	2.78e-06	32	107	5	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	5.89e-06	445	517	22	107	N-terminal domain of M60-like peptidases. This accessory domain has a jelly roll topology.
pfam13004	BACON	5.02e-05	145	205	2	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
QCT79445.1	6.12e-212	8	918	13	939
QRP89238.1	6.12e-212	8	918	13	939
QUU03487.1	1.92e-210	8	918	13	939
QRM71921.1	2.14e-209	2	918	3	939
QTO25368.1	2.14e-209	2	918	3	939

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5KD2_A	1.50e-68	366	913	25	604	BT_4244metallopeptidase from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482]
7SCI_A	7.40e-66	375	827	14	478	ChainA, Peptidase M60 domain-containing protein [Akkermansia muciniphila ATCC BAA-835]
5KD5_A	3.34e-63	407	913	20	556	BT_4244metallopeptidase from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482],5KD8_A BT_4244 metallopeptidase in complex with Tn antigen. [Bacteroides thetaiotaomicron VPI-5482]
5EV7_A	9.25e-40	445	844	45	422	Thecrystal structure of a functionally unknown conserved protein mutant from Bacillus anthracis str. Ames [Bacillus anthracis str. Ames]
4FCA_A	4.39e-38	445	844	45	422	Thecrystal structure of a functionally unknown conserved protein 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
0.000020	0.015995	0.983993	0.000006	0.000008	0.000007

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001551_03099.