CAZyme Information: MGYG000003543.1_01678

Basic Information

• Species: HGM04593 sp900769465
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; HGM04593; HGM04593 sp900769465
• CAZyme ID: MGYG000003543.1_01678
• CAZy Family: GH33
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1709	MGYG000003543.1_247|CGC2	185998.69	4.6922

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003543.1	3216165	MAG	Fiji	Oceania

• Gene Location: Start: 21448; End: 26577 Strand: -

Full Sequence      

MKRLFTLLICGLLSAATMFADEPFRNHRYDSFKVLETTGESIVFIGNSITDMHCWPEAFK
TSTGEYLPIVNRGNSGTYSTEQSNNLESYINGKPKKVFMMIGTNDIATSGGLNFSGEQVL
AYVKSIVSRIHARSPQTKIYLYSILKNNTSNRVEATWLHTNEIVKAYADATDKVTYIDLY
DKLAGVAQGGVWSYDYLHLTAAAYQVWCETICQYLQEGEDYTVTAVYPSNTSSLQQNGGL
GSAHGMRATYFSMLPISNEDVLVFGDEFIKNGEWQELLGNRNVKNRGTGWGYGGDIATTS
KIVDATYANTGVEKKDAKAIFIYTGTGDCNGSTDIATVKNSYKALVDKIAQKSPTSKIYL
MALAPTNNATTNTSRIAALNSYMQNLATGNIRYVDTYTPLLNGNVANTKYFYPSNYLGGL
GYAVMANAMTDALKADFPADTYAATSEADAEVRYAQATLRNTLSQVIARGLIMERGEAMG
QYDPEKMAAFDAELEKAYTLLEKESITESEVQAMSNSLNEVLKEALAMPKASTDTEEHWY
QFTSLRSNNLYISAEGEAAGVVGKDNTAASAVSMWKFVDRGDNTFDIVNRQYGSYLNPVA
NYNTQITTTKSRPANGWTVSYADTPAYYIISSGEVQLNQTGSGQSFKLYNWSNSATLGSD
RGDTGCQLSIFEAGEIAELPETSAKTLTLGIDQFANGASTWSKHVSTSDGWYGKFVTGTD
PALTVEGIDNNVNNIGWSQKRPWFQEGYTYTFSLPEGYLINAYELTTLDANGFNGTFTYT
TAEGTATSAAQTNTPQTVKAEGLSTRTITIKVGDGQTSTNGIMMTNLVIQYTDNGSEGEV
ANLEFTIDKANGNLYHKDGAANQNWNCCWKSNATPQLQFGCGTINNMNWSGNNVQLMTGS
VGSANYSITAPSGYVISEYSFTFANNGHNTGLELTMDNGALYTTSTTAQTISAKNQNTGS
VSFRLAGNNGNGVVLTNFTVKIKEDKIVAPKISTEGDEHWYYITSASTQTYCAGKVIYID
GDMGKLRFGDKMFSADRIWSLWEKNGKIAIKNYRGEYFGTAGSGTGNSTAFGVVNEPNYI
YNINSAYEFFVIKDNAVELHAQNDNSVIVRWGAAAGNASLWKFDEVDTSDAMADFASSRV
VQGKVSTGIGNTNQPIVRSTIRIGGLDGTVEFQGVKGSFSGTDRNDITNVKAYFATNSRE
LFVDTDKKMTWREENGEQFGETVTLAADGTFTITGNKTLVPGDNYLWITYDIAETAKEGN
TVDASIASYTIDGEEIAENNGNPAHSVTIFLSEGAVLMPMDKGSLYYRIPAITATKDGKR
LVTLTDDRKHHNTDLPSHCYLVAQYSEDNGRTWSDPVTVAGTAETGGDYGHGDASIVTNR
DNGEIVGIMTSAGTYGHGFFAGTAAEPPRWKTITSRDGGLTWETPVDHTDDLFGANCSNP
NTQTWKSGFSGSGAALQKRDGTLVSSFVNRQADNSQHFYFFMSKDGGQSWYVSGTSGTSG
ADEPKTLERNNGDLAISVRASGYNYYNYTSNDGETWHLPSQTRFNSGISGNACDGEYMVW
CSTVEGNPWDIAFQTLPNSSSRQNVSIALSTDEGATFGTPKTICPIGSAYSAAVVLPDGT
LGVYYEENGVFGGFTMRFVRFSLDWASSGTYKFTDDAPFFPIKSTNPTAIEEVKSEVGEG
KTEIYDLQGRRVTNPTKGLYIVNGKKVMF

Enzyme Prediction     

No EC number prediction in MGYG000003543.1_01678.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH33	1301	1642	2.9e-54	0.956140350877193

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd15482	Sialidase_non-viral	1.99e-61	1296	1642	3	339	Non-viral sialidases. Sialidases or neuraminidases function to bind and hydrolyze terminal sialic acid residues from various glycoconjugates, they play vital roles in pathogenesis, bacterial nutrition and cellular interactions. They have a six-bladed, beta-propeller fold with the non-viral sialidases containing 2-5 Asp-box motifs (most commonly Ser/Thr-X-Asp-[X]-Gly-X-Thr- Trp/Phe). This CD includes eubacterial and eukaryotic sialidases.
cd01841	NnaC_like	8.80e-27	40	215	1	174	NnaC (CMP-NeuNAc synthetase) _like subfamily of SGNH_hydrolases, a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles two of the three components of typical Ser-His-Asp(Glu) triad from other serine hydrolases. E. coli NnaC appears to be involved in polysaccharide synthesis.
cd01828	sialate_O-acetylesterase_like2	5.33e-25	42	216	2	169	sialate_O-acetylesterase_like subfamily of the SGNH-hydrolases, a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases.
pfam13472	Lipase_GDSL_2	4.17e-19	44	206	1	176	GDSL-like Lipase/Acylhydrolase family. This family of presumed lipases and related enzymes are similar to pfam00657.
cd01820	PAF_acetylesterase_like	4.80e-18	42	217	35	212	PAF_acetylhydrolase (PAF-AH)_like subfamily of SGNH-hydrolases. Platelet-activating factor (PAF) and PAF-AH are key players in inflammation and in atherosclerosis. PAF-AH is a calcium independent phospholipase A2 which exhibits strong substrate specificity towards PAF, hydrolyzing an acetyl ester at the sn-2 position. PAF-AH also degrades a family of oxidized PAF-like phospholipids with short sn-2 residues. In addition, PAF and PAF-AH are associated with neural migration and mammalian reproduction.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BCI63993.1	2.24e-118	1137	1654	43	544
QCX54140.1	1.68e-88	1125	1649	21	524
QKJ63384.1	1.99e-83	1227	1671	555	986
QUT75110.1	1.05e-82	1132	1682	261	791
AYN04290.1	2.96e-82	1140	1707	490	1036

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1EUR_A	9.87e-25	1307	1645	25	358	Sialidase[Micromonospora viridifaciens],1EUS_A Sialidase Complexed With 2-Deoxy-2,3-Dehydro-N- Acetylneuraminic Acid [Micromonospora viridifaciens]
1EUT_A	6.58e-24	1307	1689	25	410	Sialidase,Large 68kd Form, Complexed With Galactose [Micromonospora viridifaciens],1EUU_A Sialidase Or Neuraminidase, Large 68kd Form [Micromonospora viridifaciens]
1WCQ_A	1.98e-23	1307	1689	21	406	Mutagenesisof the Nucleophilic Tyrosine in a Bacterial Sialidase to Phenylalanine. [Micromonospora viridifaciens],1WCQ_B Mutagenesis of the Nucleophilic Tyrosine in a Bacterial Sialidase to Phenylalanine. [Micromonospora viridifaciens],1WCQ_C Mutagenesis of the Nucleophilic Tyrosine in a Bacterial Sialidase to Phenylalanine. [Micromonospora viridifaciens]
2BZD_A	3.48e-23	1307	1689	21	406	Galactoserecognition by the carbohydrate-binding module of a bacterial sialidase. [Micromonospora viridifaciens],2BZD_B Galactose recognition by the carbohydrate-binding module of a bacterial sialidase. [Micromonospora viridifaciens],2BZD_C Galactose recognition by the carbohydrate-binding module of a bacterial sialidase. [Micromonospora viridifaciens]
1W8N_A	4.60e-23	1307	1689	21	406	Contributionof the Active Site Aspartic Acid to Catalysis in the Bacterial Neuraminidase from Micromonospora viridifaciens. [Micromonospora viridifaciens],1W8O_A Contribution of the Active Site Aspartic Acid to Catalysis in the Bacterial Neuraminidase from Micromonospora viridifaciens [Micromonospora viridifaciens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q02834	4.39e-23	1307	1689	67	452	Sialidase OS=Micromonospora viridifaciens OX=1881 GN=nedA PE=1 SV=1
P15698	1.27e-15	1306	1629	53	383	Sialidase OS=Paeniclostridium sordellii OX=1505 PE=1 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
0.000329	0.998951	0.000176	0.000179	0.000172	0.000149

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003543.1_01678.