CAZyme Information: MGYG000002498_03646

Basic Information

• Species: Enterobacter sichuanensis
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Enterobacter; Enterobacter sichuanensis
• CAZyme ID: MGYG000002498_03646
• CAZy Family: CBM5
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
674		71238.93	6.7373

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002498	4685711	Isolate	Singapore	Asia

• Gene Location: Start: 37902; End: 39926 Strand: +

Full Sequence      

MKKSILSLLICAAVTSSAYAEAATKVEFAQEGVTYTAIVVKLKPGKPLLKATNTATTTAP
DELTLGDPSLVANKMFRSNKLRSTQSDELTKLDATYGFDRYMRIDIPENKSQDKAFINHA
IAELEQNPKVELVYAEAMPVSLDEYQHDNTTTPLLRQSAGNATLTATAVPDFRNLQDYLK
SSAEKRPGYYMGGVNRDGVSGYAGSDGTGVTIISTENCAWNTSHVNLPAMALSQGDRTWK
PGCGDHDSSSVGIMAGKDIGSGIRGFAWNSKVGYAAWQTNNLYNMIPLLKAGDVVQVGMQ
AESAKPAGCTKECYNPWEAQPAFFDITKALTDKGVYVIAAAGNGGLSLDDPAYNGKFDLS
VKDSGAIIVGAMCASDGKKAYFSSYGSRVTSAAWGCWDVVTTGSGDLYRDGVNNYTRSFA
GTSSANPIIAGVVASLSGIAKAHGITVTPKQMRQILQETGTPLANGDSARIGTFPDMERA
VARIMALKDGGTPAAPAPTAAAGADYTMVSPTTGVSTYPLDGSKSLNAVSFNWSVTKGAG
TFSLEEKLNGTLVKSVDSAHAYAVIPANSEGEATYTLTTTGADGRTATDSMTIKVSKPVV
PPKDDTPAKDDTPVKPAAPAYNAKIAYPTKCTKVSYDGKIWFNQWYVNPGQETPGTGGQW
GAWREQGSSNNSCK

Enzyme Prediction     

No EC number prediction in MGYG000002498_03646.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd04843	Peptidases_S8_11	5.45e-68	203	461	11	277	Peptidase S8 family domain, uncharacterized subfamily 11. This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.
cd00306	Peptidases_S8_S53	3.20e-13	208	459	8	241	Peptidase domain in the S8 and S53 families. Members of the peptidases S8 (subtilisin and kexin) and S53 (sedolisin) family include endopeptidases and exopeptidases. The S8 family has an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. Serine acts as a nucleophile, aspartate as an electrophile, and histidine as a base. The S53 family contains a catalytic triad Glu/Asp/Ser with an additional acidic residue Asp in the oxyanion hole, similar to that of subtilisin. The serine residue here is the nucleophilic equivalent of the serine residue in the S8 family, while glutamic acid has the same role here as the histidine base. However, the aspartic acid residue that acts as an electrophile is quite different. In S53, it follows glutamic acid, while in S8 it precedes histidine. The stability of these enzymes may be enhanced by calcium; some members have been shown to bind up to 4 ions via binding sites with different affinity. There is a great diversity in the characteristics of their members: some contain disulfide bonds, some are intracellular while others are extracellular, some function at extreme temperatures, and others at high or low pH values.
cd07498	Peptidases_S8_15	5.06e-12	326	459	122	242	Peptidase S8 family domain, uncharacterized subfamily 15. This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.
cd07477	Peptidases_S8_Subtilisin_subset	7.46e-12	321	459	111	229	Peptidase S8 family domain in Subtilisin proteins. This group is composed of many different subtilisins: Pro-TK-subtilisin, subtilisin Carlsberg, serine protease Pb92 subtilisin, and BPN subtilisins just to name a few. Pro-TK-subtilisin is a serine protease from the hyperthermophilic archaeon Thermococcus kodakaraensis and consists of a signal peptide, a propeptide, and a mature domain. TK-subtilisin is matured from pro-TK-subtilisin upon autoprocessing and degradation of the propeptide. Unlike other subtilisins though, the folding of the unprocessed form of pro-TK-subtilisin is induced by Ca2+ binding which is almost completed prior to autoprocessing. Ca2+ is required for activity unlike the bacterial subtilisins. The propeptide is not required for folding of the mature domain unlike the bacterial subtilases because of the stability produced from Ca2+ binding. Subtilisin Carlsberg is extremely similar in structure to subtilisin BPN'/Novo thought it has a 30% difference in amino acid sequence. The substrate binding regions are also similar and 2 possible Ca2+ binding sites have been identified recently. Subtilisin Carlsberg possesses the highest commercial importance as a proteolytic additive for detergents. Serine protease Pb92, the serine protease from the alkalophilic Bacillus strain PB92, also contains two calcium ions and the overall folding of the polypeptide chain closely resembles that of the subtilisins. Members of the peptidases S8 and S35 clan include endopeptidases, exopeptidases and also a tripeptidyl-peptidase. The S8 family has an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The S53 family contains a catalytic triad Glu/Asp/Ser. The stability of these enzymes may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.
cd07496	Peptidases_S8_13	5.96e-11	329	459	161	285	Peptidase S8 family domain, uncharacterized subfamily 13. This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QFQ10755.1	0.0	1	674	1	674
AFM61610.1	0.0	1	674	1	670
QGN44379.1	7.62e-318	1	674	1	664
QUG54103.1	2.29e-317	1	674	1	664
QCD12383.1	5.34e-317	1	674	1	664

PDB Hits     

has no PDB hit.

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P42780	1.20e-06	331	485	327	472	Extracellular subtilisin-like protease OS=Dichelobacter nodosus OX=870 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000282	0.998997	0.000205	0.000190	0.000177	0.000155

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002498_03646.