dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000001595_01204

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Basic Information help

Species

Fusobacterium_B sp900545035

Lineage

Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Fusobacteriaceae; Fusobacterium_B; Fusobacterium_B sp900545035

CAZyme ID

MGYG000001595_01204

CAZy Family

CBM50

CAZyme Description

Trifunctional nucleotide phosphoesterase protein YfkN

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
587	MGYG000001595_80\|CGC1	66057.47	5.2994

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001595	1844851	MAG	China	Asia

Gene Location

Start: 4640; End: 6403 Strand: +

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in MGYG000001595_01204.

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK09419	PRK09419	2.20e-159	1	585	5	647	multifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase/5'-nucleotidase.
COG0737	UshA	2.22e-91	4	487	1	499	2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or 3'-nucleotidase, 5'-nucleotidase family [Nucleotide transport and metabolism, Defense mechanisms].
cd07410	MPP_CpdB_N	3.50e-81	30	293	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.
PRK11907	PRK11907	2.06e-59	24	541	110	677	bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase.
PRK09418	PRK09418	2.38e-59	24	541	34	605	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	2.03e-229	23	587	31	606
AAO36497.1	1.08e-226	8	587	13	606
QBD85406.1	1.53e-226	8	587	13	606
AVP54978.1	3.07e-226	8	587	13	606
SNV84369.1	2.43e-225	2	587	7	606

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3GVE_A	2.70e-35	30	287	12	307	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]
4Q7F_A	5.46e-31	29	533	19	517	ChainA, 5' nucleotidase family protein [Staphylococcus aureus subsp. aureus COL]
3QFK_A	5.46e-31	29	533	19	517	ChainA, Uncharacterized protein [Staphylococcus aureus subsp. aureus NCTC 8325]
3IVD_A	6.18e-31	28	486	5	451	Putative5'-Nucleotidase (c4898) from Escherichia Coli in complex with Uridine [Escherichia coli O6],3IVD_B Putative 5'-Nucleotidase (c4898) from Escherichia Coli in complex with Uridine [Escherichia coli O6],3IVE_A Putative 5'-Nucleotidase (c4898) from Escherichia Coli in complex with Cytidine [Escherichia coli O6]
5EQV_A	1.34e-29	23	303	3	317	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]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O34313	8.61e-52	30	543	45	609	Trifunctional nucleotide phosphoesterase protein YfkN OS=Bacillus subtilis (strain 168) OX=224308 GN=yfkN PE=1 SV=1
P26265	1.18e-46	16	543	8	595	2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=cpdB PE=3 SV=2
P08331	3.03e-46	16	543	8	595	2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase OS=Escherichia coli (strain K12) OX=83333 GN=cpdB PE=1 SV=2
P44764	2.70e-44	25	568	29	637	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
P53052	4.77e-44	2	573	3	637	2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase OS=Yersinia enterocolitica OX=630 GN=cpdB PE=3 SV=1

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
0.000348	0.998955	0.000204	0.000156	0.000151	0.000142

TMHMM Annotations download full data without filtering help

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