CAZyme Information: MGYG000001469_01897

Basic Information

• Species: Neobacillus jeddahensis
• Lineage: Bacteria; Firmicutes; Bacilli; Bacillales_B; DSM-18226; Neobacillus; Neobacillus jeddahensis
• CAZyme ID: MGYG000001469_01897
• CAZy Family: CBM50
• CAZyme Description: 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
370	MGYG000001469_15|CGC2	41197.74	9.478

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001469	4762944	Isolate	not provided	not provided

• Gene Location: Start: 42909; End: 44021 Strand: -

Full Sequence      

MDKKKIPYLLIGCFLFWLSCSSLSFAADSTPQTMVELRILETTDLHAELVNYDYYQTKVD
NRIGLVKTATLINEARNEAKNTLLFDDGDHLKGNPLGEYLARIRGMHKGKTHPVYRAFNY
LNYDAIAIGNHEFNYGLGFLMTALKGAKMPALNANVFSVKTNKPLFTPYTILKRNVVDEN
GKQYQLNIGVIAFMPTQIMKWDKANLEGKVIAKPIVETAKEFVPIMKAKGADIIVALAHT
GISSEPYRPDSENDAYYLTIIPGIDAILSGHSHSVFPGPVFQDIKNTNLKTGQINGKPVV
MAGAFGSRLGIIDLQLWNHAGKWEIVTGKALTRPIADENGKALVKTDKGLFRLVKREHEE
TVDFIKKLGL

Enzyme Prediction     

No EC number prediction in MGYG000001469_01897.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK09420	cpdB	2.06e-174	24	367	13	356	bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase.
TIGR01390	CycNucDiestase	9.57e-157	35	367	1	333	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]
PRK09418	PRK09418	1.32e-134	26	365	29	367	bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase.
PRK11907	PRK11907	1.86e-123	28	367	105	446	bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase.
cd07410	MPP_CpdB_N	1.95e-117	37	335	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
APO43595.1	1.81e-115	26	366	28	372
QZN77538.1	2.67e-115	26	366	30	374
QLG37215.1	3.33e-115	26	366	30	374
QOS76560.1	1.56e-114	26	366	30	374
QKS58250.1	4.15e-114	3	366	4	374

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5EQV_A	3.15e-117	35	367	8	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]
3JYF_A	6.12e-117	29	367	1	339	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]
3GVE_A	6.28e-91	24	367	1	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]
5H7W_A	3.90e-17	36	322	4	274	Crystalstructure of 5'-nucleotidase from venom of Naja atra [Naja atra],5H7W_B Crystal structure of 5'-nucleotidase from venom of Naja atra [Naja atra]
7D0V_A	7.03e-17	36	322	4	274	ChainA, Snake venom 5'-nucleotidase [Naja atra],7D0V_B Chain B, Snake venom 5'-nucleotidase [Naja atra]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P26265	1.37e-118	27	367	14	354	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	3.05e-117	27	367	14	354	2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase OS=Escherichia coli (strain K12) OX=83333 GN=cpdB PE=1 SV=2
P53052	3.37e-111	18	367	10	359	2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase OS=Yersinia enterocolitica OX=630 GN=cpdB PE=3 SV=1
P44764	1.01e-104	35	367	32	364	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	7.93e-86	27	367	35	374	Trifunctional nucleotide phosphoesterase protein YfkN OS=Bacillus subtilis (strain 168) OX=224308 GN=yfkN PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as LIPO

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000561	0.432135	0.566677	0.000200	0.000215	0.000193

TMHMM  Annotations     

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