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CAZyme Information: MGYG000001551_03099

You are here: Home > Sequence: MGYG000001551_03099

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

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      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001551_03099.

CDD Domains      download full data without filtering help

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      help

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      download full data without filtering help

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      help

has no Swissprot hit.

SignalP and Lipop Annotations help

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      help

There is no transmembrane helices in MGYG000001551_03099.