CAZyme Information: MGYG000001451_00185

Basic Information

• Species: Paenibacillus_A antibioticophila
• Lineage: Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus_A; Paenibacillus_A antibioticophila
• CAZyme ID: MGYG000001451_00185
• CAZy Family: CBM50
• CAZyme Description: Trifunctional nucleotide phosphoesterase protein YfkN

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
529	MGYG000001451_1|CGC5	58930.3	4.6335

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001451	5573040	Isolate	not provided	not provided

• Gene Location: Start: 201571; End: 203160 Strand: -

Full Sequence      

MASINSINLTILHTSDIHGHLYPTDYRGPGDKPLGLAKLSRLIQKERSRSTNMLLIDNGD
LLQGTPLMYHYAKFNRQGLHPAARALNALGYDAAVLGNHEFNYGQDLLRQAISDSDCPWL
SANIVNKADGKPAFGKPYRIFELPQGVRIALLGLTTHFIPNWEEPNHIGGLSFIDVLDAA
KYWVDKIRYTEQPDAVILSYHGGFERDPITGEATEPLTGENQGYAICETIEGVDILLTGH
QHRLLDGEINGVVITQPGSAGQAIAKVELEFQATPEGGWRLSSKSSSLLLVDEADQADED
FLSLFAEDERQTQHWLDQPIGRTEGDLSIPDPFTARQADHAFTEMINWIQMEVTGAELSL
AAIFTNEARGFGELITMRDVVSNYIYPNTLKVVRMRGSDIRDMLEQTARYFEVNETGDGL
CIAPSYLEPKPQHFNYDMWEGIDYTLDISKPVGHRVVRLERHGAPLNPEASFDVVMNSYR
AGGGGNFDMLKEAPVIREIPTDMTEILADYISRAGVIQATCNHNWEVVY

Enzyme Prediction     

No EC number prediction in MGYG000001451_00185.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd07410	MPP_CpdB_N	2.43e-109	9	280	1	269	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.
COG0737	UshA	2.16e-106	7	500	25	517	2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or 3'-nucleotidase, 5'-nucleotidase family [Nucleotide transport and metabolism, Defense mechanisms].
PRK09419	PRK09419	2.15e-91	5	527	38	602	multifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase/5'-nucleotidase.
PRK09420	cpdB	7.03e-78	7	525	24	595	bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase.
TIGR01390	CycNucDiestase	1.18e-71	7	528	1	575	2',3'-cyclic-nucleotide 2'-phosphodiesterase. 2',3'-cyclic-nucleotide 2'-phosphodiesterase is a bifunctional enzyme localized to the periplasm of Gram-negative bacteria. 2',3'-cyclic-nucleotide 2'-phosphodiesters are intermediates formed during the hydrolysis of RNA by the ribonuclease I, which is also found to the periplasm, and other enzymes of the RNAse T2 family. Bacteria are unable to transport 2',3'-cyclic-nucleotides into the cytoplasm. 2',3'-cyclic-nucleotide 2'-phosphodiesterase contains 2 active sites which catalyze the reactions that convert the 2',3'-cyclic-nucleotide into a 3'-nucleotide, which is then converted into nucleic acid and phosphate. Both final products can be transported into the cytoplasm. Thus, it has been suggested that 2',3'-cyclic-nucleotide 2'-phosphodiesterase has a 'scavenging' function. Experimental evidence indicates that 2',3'-cyclic-nucleotide 2'-phosphodiesterase enables Yersinia enterocolitica O:8 to grow on 2'3'-cAMP as a sole source of carbon and energy (). [Purines, pyrimidines, nucleosides, and nucleotides, Other]

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
APT74155.1	3.25e-158	6	528	18	532
ANQ54130.1	2.61e-157	6	528	18	532
APT72575.1	2.61e-157	6	528	18	532
QTA38048.1	3.26e-157	6	528	21	539
AGB41602.1	2.09e-76	9	527	37	541

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4Q7F_A	1.11e-103	8	512	19	510	ChainA, 5' nucleotidase family protein [Staphylococcus aureus subsp. aureus COL]
3QFK_A	1.11e-103	8	512	19	510	ChainA, Uncharacterized protein [Staphylococcus aureus subsp. aureus NCTC 8325]
5EQV_A	3.39e-41	2	296	3	313	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]
3GVE_A	3.47e-41	7	288	10	310	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]
3JYF_A	7.98e-38	3	286	1	301	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     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O34313	1.79e-68	7	527	43	609	Trifunctional nucleotide phosphoesterase protein YfkN OS=Bacillus subtilis (strain 168) OX=224308 GN=yfkN PE=1 SV=1
P53052	3.07e-64	2	527	22	600	2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase OS=Yersinia enterocolitica OX=630 GN=cpdB PE=3 SV=1
P26265	2.02e-61	2	527	15	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	1.04e-60	2	527	15	595	2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase OS=Escherichia coli (strain K12) OX=83333 GN=cpdB PE=1 SV=2
P44764	1.94e-53	5	528	30	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

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
1.000055	0.000003	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001451_00185.