CAZyme Information: MGYG000001702_02568

Basic Information

• Species: Virgibacillus picturae
• Lineage: Bacteria; Firmicutes; Bacilli; Bacillales_D; Amphibacillaceae; Virgibacillus; Virgibacillus picturae
• CAZyme ID: MGYG000001702_02568
• CAZy Family: CBM50
• CAZyme Description: Trifunctional nucleotide phosphoesterase protein YfkN

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
525	MGYG000001702_2|CGC3	59014.57	5.4478

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001702	3675175	Isolate	Saudi Arabia	Asia

• Gene Location: Start: 307835; End: 309412 Strand: -

Full Sequence      

MKKHEEASLTLLYTSDVHGNAMPISYATNEYSDSGLAKYATAVKQVRKEKDYVLVLDNGD
LIQGTPFMTHYVKQHRHTENPMITIMNQIGIDGAVIGNHEFNFGSDVLSDAVEQSQFPWL
SANIIDTVTNKPKYGPAYIMKTLPNGIKVAITGVTTHYIPNWESPEHIEGLYFADAYETL
KKWTTYIRQTEEPDILIASYHGGFERDLETGHETEALTGENQGYRMCDIEGIDVLLTGHQ
HRKLTGKVNDVLVIQPGNNGTLYGEINLSLSNASGKWIIKEKEAHLRDLTSVPADNEALQ
AIEALEASTQNWLDEPIGFIKGDMTIHDPFQVRISKHPFIEFIQKVQMEESGVDISVTSL
LNNTSKGFSSSVTMRDVVSNYMYPNTLVVLKLTGEDIKKALEKSAEYFTLIDGDIAVNPA
FETPKPQHYNYDMWEGIQYSISVNEPVGNRVKDISYHGKPIAYDESYHVVLNNYRATGGG
NYDMFKEKPVVKEIQKDAVEIIRSYFERHKTVKATATPNFVVKAK

Enzyme Prediction     

No EC number prediction in MGYG000001702_02568.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG0737	UshA	6.62e-111	1	495	19	517	2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or 3'-nucleotidase, 5'-nucleotidase family [Nucleotide transport and metabolism, Defense mechanisms].
cd07410	MPP_CpdB_N	1.10e-97	9	287	1	278	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	1.71e-85	4	520	37	600	multifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase/5'-nucleotidase.
PRK09420	cpdB	2.07e-68	7	479	24	551	bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase.
PRK11907	PRK11907	8.05e-61	5	520	112	677	bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ANQ54130.1	1.83e-172	9	520	21	529
APT72575.1	1.83e-172	9	520	21	529
QTA38048.1	6.29e-167	5	520	20	536
APT74155.1	1.85e-164	9	520	21	529
AGB41602.1	1.49e-81	8	522	36	541

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3QFK_A	2.16e-115	7	522	18	525	ChainA, Uncharacterized protein [Staphylococcus aureus subsp. aureus NCTC 8325]
4Q7F_A	2.16e-115	7	522	18	525	ChainA, 5' nucleotidase family protein [Staphylococcus aureus subsp. aureus COL]
5EQV_A	1.17e-33	9	315	10	340	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	1.65e-33	6	314	9	337	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]
1HP1_A	1.46e-31	9	508	9	498	5'-Nucleotidase(Open Form) Complex With Atp [Escherichia coli]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O34313	4.90e-59	6	522	42	609	Trifunctional nucleotide phosphoesterase protein YfkN OS=Bacillus subtilis (strain 168) OX=224308 GN=yfkN PE=1 SV=1
P08331	1.66e-55	9	479	24	549	2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase OS=Escherichia coli (strain K12) OX=83333 GN=cpdB PE=1 SV=2
P26265	6.06e-55	9	479	24	549	2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=cpdB PE=3 SV=2
P53052	6.03e-53	9	479	29	554	2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase OS=Yersinia enterocolitica OX=630 GN=cpdB PE=3 SV=1
P44764	1.96e-49	2	519	27	598	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
1.000061	0.000003	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001702_02568.