dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000001300_01209

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Basic Information help

Species

Faecalibacterium prausnitzii

Lineage

Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; Faecalibacterium; Faecalibacterium prausnitzii

CAZyme ID

MGYG000001300_01209

CAZy Family

CBM50

CAZyme Description

Trifunctional nucleotide phosphoesterase protein YfkN

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
603	MGYG000001300_3\|CGC1	66519.64	5.3021

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001300	3126983	Isolate	not provided	not provided

Gene Location

Start: 83311; End: 85122 Strand: +

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in MGYG000001300_01209.

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK09419	PRK09419	1.94e-144	5	597	3	644	multifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase/5'-nucleotidase.
COG0737	UshA	9.37e-88	17	512	5	510	2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or 3'-nucleotidase, 5'-nucleotidase family [Nucleotide transport and metabolism, Defense mechanisms].
cd07410	MPP_CpdB_N	9.10e-82	44	308	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.
PRK09420	cpdB	1.06e-64	19	558	9	598	bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase.
PRK11907	PRK11907	4.63e-60	17	555	84	677	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	4.17e-189	41	600	35	605
QBD85406.1	6.72e-188	41	600	35	605
AAO36497.1	9.51e-188	41	600	35	605
AVP54978.1	1.90e-187	41	600	35	605
SNV84369.1	2.78e-184	41	603	35	608

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3GVE_A	1.50e-34	44	300	12	305	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	1.13e-30	43	499	19	479	ChainA, 5' nucleotidase family protein [Staphylococcus aureus subsp. aureus COL]
3QFK_A	1.13e-30	43	499	19	479	ChainA, Uncharacterized protein [Staphylococcus aureus subsp. aureus NCTC 8325]
5EQV_A	2.35e-28	41	319	7	318	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	1.40e-25	41	304	6	302	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
P44764	4.39e-49	42	558	32	606	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
O34313	1.97e-48	44	557	45	609	Trifunctional nucleotide phosphoesterase protein YfkN OS=Bacillus subtilis (strain 168) OX=224308 GN=yfkN PE=1 SV=1
P53052	1.57e-41	41	561	26	604	2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase OS=Yersinia enterocolitica OX=630 GN=cpdB PE=3 SV=1
P08331	2.77e-41	41	557	21	595	2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase OS=Escherichia coli (strain K12) OX=83333 GN=cpdB PE=1 SV=2
P26265	5.03e-39	41	557	21	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

SignalP and Lipop Annotations help

This protein is predicted as TAT

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000000	0.000001	0.000001	0.973018	0.026959	0.000000

TMHMM Annotations help

There is no transmembrane helices in MGYG000001300_01209.