CAZyme Information: MGYG000000642_00183

Basic Information

• Lineage: Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Actinomycetaceae; Arcanobacterium_A
• CAZyme ID: MGYG000000642_00183
• CAZy Family: GH33
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1752	MGYG000000642_1|CGC3	191042.85	5.2479

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000642	1644124	MAG	Madagascar	Africa

• Gene Location: Start: 205799; End: 211057 Strand: -

Full Sequence      

MGKFGKALASITGAALGLSAITMSILEVPQANAAEGEFTHTTVVKYGDASITNYRIPAVI
KLKNGDLLVSYDARPANGDAPAPNSIMQKRSTDGGKTWGEQTTIAAGKGTTMNAPDKEGF
SDPAYIYDETTNTIFNFHVHSYDAGCNQNGSTGTDEFTDRNVQGVSLSVSTDNGVTWKER
HGSTEDTDRGLTADVKQPGYPCGFASSGHGIQLKHQTGANESKNGRLITQFIAGKGNEWA
AYSVYSDDHGKTWKRGATIGTDMNENKLVELSDGTLLLNSRMSSKGGYRHIAKSTDGGET
WSSLELERSLIDSKTPGRNASIVRMYPEASASDPKSKELLYSGMAESGKTLAVSYSYDDG
ATWPIRKLYWNNKAAYSDLVVIDAEKGQYGVAFEEDHQVGNNWFETIHFGTFDKTWLNPV
KVSLADATIEAEAGTTVEIPITIKNDDSGDTKIPVGTPVKLNLPQGWTMEESVLAQDLYP
NNSETVTLRVSIPANASQQTYYFDSVLESSNIKLRGDVNVNVTNSNIVTDPTKSVGVTFE
LTNPKSDGTWAVGEKMNFTVNVTNMMGQDKSFTATASNLDNGWEGCKWRSLSAGATLPCA
NRTHTVTQADIDAGGFTPSITFKYQNTGYSGAATQLEAVQGKQSPVYARHVKITDLKVKG
TKNSYAVGDKITFTPTVQNIGNTPIDVQLTGENFTLSCQNENGKLAKDATFSCTSSDYSL
KSADIAQGNFTPKVKVKVTDGTKVLQEFTYAGESIPLPSDDPIATKLPQTIPSLDSWKAN
LDANAVFELTAQTKVYYPAGFESQAKIIAQELNAYLKAAGLAETVTAQASDGAKSEINDI
TISIDEAQKTKLGEEGYQLTIGETGVQISAAAKRGAFWGTRTVSQMLRQQLKLPFGNATD
KPQQTERAVTLCACRIKNQPDYIERMLTDMADLRMNQVILTAKMQSNKEPVTNTYSYYSK
EELKDIVAFADTLGIEIVPQMGAPGHMDPKIHNLPQYQLKKTDGTLDSDRLDITNPEAVA
FYKRQIDDYLDVFPSKYWHMAGDEYMYRSSYSNYPVFGEKGKDGARLFVEFVNDINKYVK
SKGKTLRMWNDGLNASNIDQLDKDIVIDMWQNGLSPQSLIDKGHKVNNTNYDLYFSREMG
WRIQNNGAATIYNDRGFTAGTFKSGKVADNNTNNLGIKLSIWPDTSIYQTENEVEMETFD
AFRLVSQIGWSGSRPWKDGATFVDFAKKLGRNPLWENVNRKPLENGTYAFTAEGLRLDGS
ENREPDAIAYSDDQWEIKSTYDHYYQLKSKASGKCLTMDVGKHNLNGSKRQYATTDLTVV
NEVGARPALVDCVADMDVKYHTGTWKNNSSTSIRNNQKWQIIADNNGRYIVRHALTNMDL
AISTGEEKHVDLGNVGDMDDNAKSRPMPTDLIQLPSDMTNTRWSITPADRDAAPNMQKPH
GKGVSVANLPWYDGSTIGWADDGLIRVNRTLLGSPLLIGGEKYRSGIGTHASSKITVHLG
KNCTSFSAKVGIDDTQKDTKNKNADGVIFRVLGADGSELGASSQQKPGEKAQELKVSVEN
QEKITLFADAGNSNGNDHADWADAVVNCNEMDADKYQPAYADAQAKAGETATTAVPSFTA
SEGKAKAKKFEFAETAPANMSIAEDSGAITWKVPSDHVNETISVSVKVTYEDGSNEIVTA
NFQVVAAMPTPQPEQQPGEDNPSEKESPQKPTEPIVNKQLQKTGSATAGLIALAVLLSVA
GGALLTSKKRIW

Enzyme Prediction     

EC	3.2.1.18	3.2.1.-

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH33	42	406	2.7e-74	0.9532163742690059
GH20	906	1212	1.3e-51	0.9525222551928784
CBM51	1446	1585	8e-32	0.9701492537313433

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd15482	Sialidase_non-viral	5.85e-84	41	413	1	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.
cd06564	GH20_DspB_LnbB-like	5.95e-62	906	1212	2	326	Glycosyl hydrolase family 20 (GH20) catalytic domain of dispersin B (DspB), lacto-N-biosidase (LnbB) and related proteins. Dispersin B is a soluble beta-N-acetylglucosamidase found in bacteria that hydrolyzes the beta-1,6-linkages of PGA (poly-beta-(1,6)-N-acetylglucosamine), a major component of the extracellular polysaccharide matrix. Lacto-N-biosidase hydrolyzes lacto-N-biose (LNB) type I oligosaccharides at the nonreducing terminus to produce lacto-N-biose as part of the GNB/LNB (galacto-N-biose/lacto-N-biose I) degradation pathway. The lacto-N-biosidase from Bifidobacterium bifidum has this GH20 domain, a carbohydrate binding module 32, and a bacterial immunoglobulin-like domain 2, as well as a YSIRK signal peptide and a G5 membrane anchor at the N and C termini, respectively. The GH20 hexosaminidases are thought to act via a catalytic mechanism in which the catalytic nucleophile is not provided by solvent or the enzyme, but by the substrate itself.
pfam08305	NPCBM	5.29e-33	1444	1586	3	135	NPCBM/NEW2 domain. This novel putative carbohydrate binding module (NPCBM) domain is found at the N-terminus of glycosyl hydrolase family 98 proteins. This domain has also been called the NEW2 domain (Naumoff DG. Phylogenetic analysis of alpha-galactosidases of the GH27 family. Molecular Biology (Engl Transl). (2004)38:388-399.)
pfam00728	Glyco_hydro_20	8.90e-26	920	1135	17	267	Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
cd06563	GH20_chitobiase-like	4.99e-25	957	1229	82	357	The chitobiase of Serratia marcescens is a beta-N-1,4-acetylhexosaminidase with a glycosyl hydrolase family 20 (GH20) domain that hydrolyzes the beta-1,4-glycosidic linkages in oligomers derived from chitin. Chitin is degraded by a two step process: i) a chitinase hydrolyzes the chitin to oligosaccharides and disaccharides such as di-N-acetyl-D-glucosamine and chitobiose, ii) chitobiase then further degrades these oligomers into monomers. This GH20 domain family includes an N-acetylglucosamidase (GlcNAcase A) from Pseudoalteromonas piscicida and an N-acetylhexosaminidase (SpHex) from Streptomyces plicatus. SpHex lacks the C-terminal PKD (polycystic kidney disease I)-like domain found in the chitobiases. The GH20 hexosaminidases are thought to act via a catalytic mechanism in which the catalytic nucleophile is not provided by solvent or the enzyme, but by the substrate itself.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AWG03116.1	6.76e-163	724	1539	264	1078
AZR04729.1	6.76e-163	724	1539	264	1078
AZR07627.1	6.76e-163	724	1539	264	1078
AWG15845.1	6.76e-163	724	1539	264	1078
QIU85951.1	5.43e-161	607	1539	164	1072

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4H04_A	1.85e-134	762	1420	28	643	Lacto-N-biosidasefrom Bifidobacterium bifidum [Bifidobacterium bifidum JCM 1254],4H04_B Lacto-N-biosidase from Bifidobacterium bifidum [Bifidobacterium bifidum JCM 1254],4JAW_A Crystal Structure of Lacto-N-Biosidase from Bifidobacterium bifidum complexed with LNB-thiazoline [Bifidobacterium bifidum JCM 1254],4JAW_B Crystal Structure of Lacto-N-Biosidase from Bifidobacterium bifidum complexed with LNB-thiazoline [Bifidobacterium bifidum JCM 1254],5BXP_A LNBase in complex with LNB-LOGNAc [Bifidobacterium bifidum JCM 1254],5BXP_B LNBase in complex with LNB-LOGNAc [Bifidobacterium bifidum JCM 1254],5BXR_A LNBase in complex with LNB-NHAcDNJ [Bifidobacterium bifidum JCM 1254],5BXR_B LNBase in complex with LNB-NHAcDNJ [Bifidobacterium bifidum JCM 1254],5BXS_A LNBase in complex with LNB-NHAcCAS [Bifidobacterium bifidum JCM 1254],5BXS_B LNBase in complex with LNB-NHAcCAS [Bifidobacterium bifidum JCM 1254],5BXT_A LNBase in complex with LNB-NHAcAUS [Bifidobacterium bifidum JCM 1254],5BXT_B LNBase in complex with LNB-NHAcAUS [Bifidobacterium bifidum JCM 1254]
1EUT_A	2.60e-86	38	510	9	447	Sialidase,Large 68kd Form, Complexed With Galactose [Micromonospora viridifaciens],1EUU_A Sialidase Or Neuraminidase, Large 68kd Form [Micromonospora viridifaciens]
1WCQ_A	7.93e-86	38	510	5	443	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	1.46e-85	38	510	5	443	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	1.98e-85	38	510	5	443	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	1.63e-85	24	510	37	489	Sialidase OS=Micromonospora viridifaciens OX=1881 GN=nedA PE=1 SV=1
B2UPR7	1.19e-20	832	1130	164	485	Beta-hexosaminidase Amuc_2136 OS=Akkermansia muciniphila (strain ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC 81048 / CCUG 64013 / CIP 107961 / Muc) OX=349741 GN=Amuc_2136 PE=1 SV=1
P49610	4.28e-16	921	1135	226	470	Beta-N-acetylhexosaminidase OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=strH PE=1 SV=2
A9WNA0	5.82e-14	1436	1588	1155	1305	Putative endo-alpha-N-acetylgalactosaminidase OS=Renibacterium salmoninarum (strain ATCC 33209 / DSM 20767 / JCM 11484 / NBRC 15589 / NCIMB 2235) OX=288705 GN=RSal33209_1326 PE=3 SV=2
P13723	1.05e-13	834	1126	80	391	Beta-hexosaminidase subunit A1 OS=Dictyostelium discoideum OX=44689 GN=hexa1 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
0.000424	0.998725	0.000191	0.000250	0.000220	0.000180

TMHMM  Annotations     

start	end
1723	1745