dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000002356_05150

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Basic Information help

Species

Bacillus_A wiedmannii

Lineage

Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae_G; Bacillus_A; Bacillus_A wiedmannii

CAZyme ID

MGYG000002356_05150

CAZy Family

CBM50

CAZyme Description

Trifunctional nucleotide phosphoesterase protein YfkN

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
648	MGYG000002356_47\|CGC4	72135.51	8.5719

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002356	5414628	Isolate	Netherlands	Europe

Gene Location

Start: 311848; End: 313794 Strand: -

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in MGYG000002356_05150.

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd07410	MPP_CpdB_N	5.99e-116	39	306	1	280	Escherichia coli CpdB and related proteins, N-terminal metallophosphatase domain. CpdB is a bacterial periplasmic protein with an N-terminal metallophosphatase domain and a C-terminal 3'-nucleotidase domain. This alignment model represents the N-terminal metallophosphatase domain, which has 2',3'-cyclic phosphodiesterase activity, hydrolyzing the 2',3'-cyclic phosphates of adenosine, guanosine, cytosine and uridine to yield nucleoside and phosphate. CpdB also hydrolyzes the chromogenic substrates p-nitrophenyl phosphate (PNPP), bis(PNPP) and p-nitrophenyl phosphorylcholine (NPPC). CpdB is thought to play a scavenging role during RNA hydrolysis by converting the non-transportable nucleotides produced by RNaseI to nucleosides which can easily enter a cell for use as a carbon source. This family also includes YfkN, a Bacillus subtilis nucleotide phosphoesterase with two copies of each of the metallophosphatase and 3'-nucleotidase domains. The N-terminal metallophosphatase domain belongs to a large superfamily of distantly related metallophosphatases (MPPs) that includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.
PRK09419	PRK09419	2.23e-114	14	605	17	643	multifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase/5'-nucleotidase.
COG0737	UshA	4.33e-89	14	483	3	475	2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or 3'-nucleotidase, 5'-nucleotidase family [Nucleotide transport and metabolism, Defense mechanisms].
PRK09419	PRK09419	3.02e-54	32	566	653	1144	multifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase/5'-nucleotidase.
PRK09418	PRK09418	4.82e-52	16	571	13	611	bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CDI50173.1	1.82e-172	2	609	3	604
QBD85406.1	1.03e-171	2	609	3	604
AAO36497.1	1.64e-170	2	609	3	604
AVP54978.1	1.31e-169	2	609	3	604
SNV84369.1	2.42e-158	2	609	3	604

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3GVE_A	4.40e-35	30	329	1	333	Crystalstructure of calcineurin-like phosphoesterase YfkN from Bacillus subtilis [Bacillus subtilis subsp. subtilis str. 168],3GVE_B Crystal structure of calcineurin-like phosphoesterase YfkN from Bacillus subtilis [Bacillus subtilis subsp. subtilis str. 168]
3QFK_A	3.03e-28	38	506	19	478	ChainA, Uncharacterized protein [Staphylococcus aureus subsp. aureus NCTC 8325]
4Q7F_A	3.03e-28	38	506	19	478	ChainA, 5' nucleotidase family protein [Staphylococcus aureus subsp. aureus COL]
5EQV_A	4.45e-27	30	306	1	307	1.45Angstrom Crystal Structure of Bifunctional 2',3'-cyclic Nucleotide 2'-phosphodiesterase/3'-Nucleotidase Periplasmic Precursor Protein from Yersinia pestis with Phosphate bound to the Active site [Yersinia pestis CO92]
3JYF_A	1.01e-24	31	306	1	306	ChainA, 2',3'-cyclic nucleotide 2'-phosphodiesterase/3'-nucleotidase bifunctional periplasmic protein [Klebsiella pneumoniae subsp. pneumoniae MGH 78578],3JYF_B Chain B, 2',3'-cyclic nucleotide 2'-phosphodiesterase/3'-nucleotidase bifunctional periplasmic protein [Klebsiella pneumoniae subsp. pneumoniae MGH 78578]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O34313	6.25e-46	18	571	22	613	Trifunctional nucleotide phosphoesterase protein YfkN OS=Bacillus subtilis (strain 168) OX=224308 GN=yfkN PE=1 SV=1
P44764	2.30e-34	20	570	15	608	2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase OS=Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) OX=71421 GN=cpdB PE=3 SV=1
P08331	1.32e-32	30	570	15	598	2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase OS=Escherichia coli (strain K12) OX=83333 GN=cpdB PE=1 SV=2
P53052	2.53e-31	30	572	20	605	2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase OS=Yersinia enterocolitica OX=630 GN=cpdB PE=3 SV=1
Q8DFG4	4.32e-30	26	473	25	493	5'-nucleotidase OS=Vibrio vulnificus (strain CMCP6) OX=216895 GN=nutA PE=3 SV=2

SignalP and Lipop Annotations help

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000359	0.998944	0.000213	0.000168	0.000158	0.000142

TMHMM Annotations download full data without filtering help

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