CAZyme Information: MGYG000001405_01123

Basic Information

• Species: Ferdinandcohnia timonensis
• Lineage: Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae_L; Ferdinandcohnia; Ferdinandcohnia timonensis
• CAZyme ID: MGYG000001405_01123
• CAZy Family: CBM50
• CAZyme Description: Trifunctional nucleotide phosphoesterase protein YfkN

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
521	MGYG000001405_1|CGC7	58832.77	4.7369

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001405	4608762	Isolate	not provided	not provided

• Gene Location: Start: 1123916; End: 1125481 Strand: -

Full Sequence      

MKSITITILETSDIHGNIFPINYGSNDKAELGLGKIATVIKQERRRNRNTIVIDNGDLIQ
GTPLTYHYVRSNSHKPNPMIALLNDLHYDAAVVGNHEFNYGMDVLQKAINESNFPWLSAN
ILNEKGEPFIGKPYLLIELEDGVKAAILGVTTHYIPNWENPEHIKGLTFDDALESTKKWV
EKIRTEENPDIMIVSYHGGFEADLETGEPTEKLTGENQGYRICTEIEGIDLLLTGHQHRS
LSGKVNGVPIVQPSFNGQAIGKATITLMRNEDMWTITESKPELIFVNEIEADEASLQLVK
EYEYETQEWLDKPIGQVIGNMTIDDPLKARLKDNALVEFINKVQMEVAKVSISNTALFNN
VTKGFPSNITMRDVVSNYIYPNTLTVIRISGKDLKEALERSASYFILENGEVTVNPSFTT
PKPQHYNYDMWEGIDYIFDLTKPIGERVVRLSFKGNPVRPDGEYDVVMNNYRAGGGGEYV
MFKDKPIIKDIPLDMSELIANYILERGTIEATVNNNWKVIW

Enzyme Prediction     

No EC number prediction in MGYG000001405_01123.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd07410	MPP_CpdB_N	8.96e-120	6	284	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.
COG0737	UshA	7.35e-119	4	492	25	517	2',3'-cyclic-nucleotide 2'-phosphodiesterase/5'- or 3'-nucleotidase, 5'-nucleotidase family [Nucleotide transport and metabolism, Defense mechanisms].
PRK09419	PRK09419	2.27e-105	3	520	39	603	multifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase/5'-nucleotidase.
PRK09420	cpdB	1.41e-88	8	518	28	596	bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase.
TIGR01390	CycNucDiestase	4.17e-86	4	518	1	573	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	3.28e-205	3	520	18	532
ANQ54130.1	1.87e-199	3	520	18	532
APT72575.1	1.87e-199	3	520	18	532
QTA38048.1	1.10e-197	2	520	20	539
AGB41602.1	7.53e-96	5	519	36	541

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4Q7F_A	1.03e-108	6	503	20	509	ChainA, 5' nucleotidase family protein [Staphylococcus aureus subsp. aureus COL]
3QFK_A	1.03e-108	6	503	20	509	ChainA, Uncharacterized protein [Staphylococcus aureus subsp. aureus NCTC 8325]
3GVE_A	8.44e-44	6	312	12	341	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]
3IVD_A	2.76e-40	6	484	7	461	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	2.86e-39	3	282	7	303	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     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O34313	2.47e-73	6	519	45	609	Trifunctional nucleotide phosphoesterase protein YfkN OS=Bacillus subtilis (strain 168) OX=224308 GN=yfkN PE=1 SV=1
P08331	5.63e-70	3	519	21	595	2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase OS=Escherichia coli (strain K12) OX=83333 GN=cpdB PE=1 SV=2
P26265	1.16e-66	3	519	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
P53052	1.82e-63	3	519	26	600	2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase OS=Yersinia enterocolitica OX=630 GN=cpdB PE=3 SV=1
P44764	2.64e-58	2	520	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
1.000038	0.000023	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001405_01123.