CAZyme Information: MGYG000004451_00561

Basic Information

• Species: CAG-313 sp003539625
• Lineage: Bacteria; Firmicutes; Bacilli; ML615J-28; CAG-313; CAG-313; CAG-313 sp003539625
• CAZyme ID: MGYG000004451_00561
• CAZy Family: GH3
• CAZyme Description: Beta-N-acetylglucosaminidase/beta-glucosidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
455	MGYG000004451_3|CGC1	51610.53	5.8277

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004451	1583580	MAG	Israel	Asia

• Gene Location: Start: 17914; End: 19281 Strand: -

Full Sequence      

MLKRLITKIKKVNHPVLVASDMEAGPVTAIVGATEFPSIRAICETEEERLAYETGKIAAI
ESREALYDWTFGPCVDILKNHFSPITSIRSASEDYKEVIKYTKQYILGLHDNGLIATAKH
FPGDGACLFDHHLTTPINPLSKEEWNNSYKKVYEEIINSNIKSIMIGHIALPCYDEKDEE
TNLYPPATLSYRLMTKLLKDELGFEGLIISDATEMSGFCGYINYYEACARFLMSGGDCLL
FAHPDEEFIMKMSELIDKGILKLDILVNRAYRVISFVNDCYNISTNIKFDIEEHQKIARE
VVEKSVKVYRDRKNILPLSKKYLKIAHIVIAKQIKTDIIGEFTNELAKYAEVTEFIDPGC
SAIKNLAKSKVYDAIICTIGCSQWYGTNQITLSGTVARNMMNGWMKYETPTIFVDFGNPY
IHEEYDAMIDTLIYTYGYAKDSCRVVAKKIFGVSE

Enzyme Prediction     

No EC number prediction in MGYG000004451_00561.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH3	8	240	3.5e-45	0.9814814814814815

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG1472	BglX	1.19e-50	2	343	46	372	Periplasmic beta-glucosidase and related glycosidases [Carbohydrate transport and metabolism].
pfam00933	Glyco_hydro_3	6.22e-48	15	275	67	315	Glycosyl hydrolase family 3 N terminal domain.
PRK05337	PRK05337	1.05e-26	2	240	42	278	beta-hexosaminidase; Provisional
cd08954	KR_1_FAS_SDR_x	4.79e-04	119	286	37	206	beta-ketoacyl reductase (KR) domain of fatty acid synthase (FAS), subgroup 1, complex (x) SDRs. NADP-dependent KR domain of the multidomain type I FAS, a complex SDR family. This subfamily also includes proteins identified as polyketide synthase (PKS), a protein with related modular protein architecture and similar function. It includes the KR domains of mammalian and chicken FAS, and Dictyostelium discoideum putative polyketide synthases (PKSs). These KR domains contain two subdomains, each of which is related to SDR Rossmann fold domains. However, while the C-terminal subdomain has an active site similar to the other SDRs and a NADP-binding capability, the N-terminal SDR-like subdomain is truncated and lacks these functions, serving a supportive structural role. In some instances, such as porcine FAS, an enoyl reductase (a Rossman fold NAD-binding domain of the medium-chain dehydrogenase/reductase, MDR family) module is inserted between the sub-domains. Fatty acid synthesis occurs via the stepwise elongation of a chain (which is attached to acyl carrier protein, ACP) with 2-carbon units. Eukaryotic systems consists of large, multifunctional synthases (type I) while bacterial, type II systems, use single function proteins. Fungal fatty acid synthesis uses a dodecamer of 6 alpha and 6 beta subunits. In mammalian type FAS cycles, ketoacyl synthase forms acetoacetyl-ACP which is reduced by the NADP-dependent beta-ketoacyl reductase (KR), forming beta-hydroxyacyl-ACP, which is in turn dehydrated by dehydratase to a beta-enoyl intermediate, which is reduced by NADP-dependent beta-enoyl reductase (ER); this KR and ER are members of the SDR family. This KR subfamily has an active site tetrad with a similar 3D orientation compared to archetypical SDRs, but the active site Lys and Asn residue positions are swapped. The characteristic NADP-binding is typical of the multidomain complex SDRs, with a GGXGXXG NADP binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type KRs have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QEN05915.1	1.65e-131	18	452	72	512
AYB42803.1	9.00e-116	2	452	57	521
BBI32796.1	2.25e-111	15	455	69	516
QYY35641.1	4.03e-111	3	452	61	524
CQR51526.1	3.87e-107	15	452	69	516

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5VQD_A	5.94e-42	15	454	86	548	Beta-glucosidephosphorylase BglX [unidentified],5VQE_A Beta-glucoside phosphorylase BglX bound to 2FGlc [unidentified]
3BMX_A	3.32e-28	15	438	117	583	Beta-N-hexosaminidase(YbbD) from Bacillus subtilis [Bacillus subtilis],3BMX_B Beta-N-hexosaminidase (YbbD) from Bacillus subtilis [Bacillus subtilis],3NVD_A Structure of YBBD in complex with pugnac [Bacillus subtilis],3NVD_B Structure of YBBD in complex with pugnac [Bacillus subtilis]
6K5J_A	1.22e-27	13	247	75	304	Structureof a glycoside hydrolase family 3 beta-N-acetylglucosaminidase from Paenibacillus sp. str. FPU-7 [Paenibacillaceae]
3LK6_A	1.35e-27	15	438	91	557	ChainA, Lipoprotein ybbD [Bacillus subtilis],3LK6_B Chain B, Lipoprotein ybbD [Bacillus subtilis],3LK6_C Chain C, Lipoprotein ybbD [Bacillus subtilis],3LK6_D Chain D, Lipoprotein ybbD [Bacillus subtilis]
4GYJ_A	1.49e-27	15	438	121	587	Crystalstructure of mutant (D318N) bacillus subtilis family 3 glycoside hydrolase (nagz) in complex with glcnac-murnac (space group P1) [Bacillus subtilis subsp. subtilis str. 168],4GYJ_B Crystal structure of mutant (D318N) bacillus subtilis family 3 glycoside hydrolase (nagz) in complex with glcnac-murnac (space group P1) [Bacillus subtilis subsp. subtilis str. 168],4GYK_A Crystal structure of mutant (D318N) bacillus subtilis family 3 glycoside hydrolase (nagz) in complex with glcnac-murnac (space group P1211) [Bacillus subtilis subsp. subtilis str. 168],4GYK_B Crystal structure of mutant (D318N) bacillus subtilis family 3 glycoside hydrolase (nagz) in complex with glcnac-murnac (space group P1211) [Bacillus subtilis subsp. subtilis str. 168]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q7WUL3	8.08e-42	15	437	84	528	Beta-N-acetylglucosaminidase/beta-glucosidase OS=Cellulomonas fimi OX=1708 GN=nag3 PE=1 SV=1
P40406	1.82e-27	15	438	117	583	Beta-hexosaminidase OS=Bacillus subtilis (strain 168) OX=224308 GN=nagZ PE=1 SV=1
P44955	1.13e-24	2	255	42	292	Beta-hexosaminidase OS=Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) OX=71421 GN=nagZ PE=3 SV=1
B8F5N0	1.77e-24	2	255	40	286	Beta-hexosaminidase OS=Glaesserella parasuis serovar 5 (strain SH0165) OX=557723 GN=nagZ PE=3 SV=1
Q6D674	8.69e-24	2	255	42	292	Beta-hexosaminidase OS=Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) OX=218491 GN=nagZ PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000046	0.000001	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000004451_00561.